MHC Class I Antibody (YA3322)

(Synonyms: Aw-68; HLA class I histocompatibility antigen; A-28 alpha chain; MHC class I antigen A*68; HLA-A; MHC class I antigen HLA A heavy chain)
Customer Review

Based on 1 Customer Validation

MHC Class I Antibody (YA3322) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to MHC Class I.

For research use only. We do not sell to patients.
  • Host:

    Rabbit

  • Isotype:

    IgG

  • Application:

    WB, IHC-P

  • Reactivity :

    Human

  • Formulation:

    Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA

  • Conjugation:
    Non-conjugated

Applications

Application
WB Info
WB: Western Blot
IHC-P Info
IHC-P: Immunohistochemistry-Paraffin
Dilution Ratio 1:500-1:1000 1:50-1:100

Product Details

Description

MHC Class I Antibody (YA3322) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to MHC Class I.

  • Host Rabbit
  • Clonality Recombinant,Monoclonal
  • Species Reactivity
    Human
  • Observed Molecular Weight
    Observed band size: 41 kDa Info
    Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
  • Calculated Molecular Weight Predicted band size: 41 kDa
Species Reactivity Database

Entrez Gene: 3105 Human

SwissProt: P04439 Human

Immunogen

A synthesized peptide derived from human MHC class I

Sensitivity

Endogenous

Purification

Affinity Purified

Conjugation

Non-conjugated

Modification

Unmodified

Isotype

IgG

RRID

AB_3105685

Product Properties

  • Appearance

    Solution

  • Formulation

    Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% BSA

  • Concentration

    Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration

  • Storage & Stability

    Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.

  • Shipping

    Shipping with blue ice.

Verification Images

  • Experimental Validation Results for MHC Class I Antibody (YA3322)
    Western blot analysis of extracts from A431 (lane2, 20μg), Jurkat (lane3, 20μg), Raji (lane4, 20μg) and HL-60 (lane5, 20μg) using MHC Class I Antibody (HY-P83577). Proteins were transferred to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80993, 1/10,000) was used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Rabbit IgG-HRP Secondary Antibody (HY-P8001,1/10,000) was used for 1 hour at room temperature.
  • Experimental Validation Results for MHC Class I Antibody (YA3322)
    Immunohistochemical analysis of paraffin-embedded human colon cancer using MHC Class I antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P83577, 1/100) for 1 hour at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
  • Experimental Validation Results for MHC Class I Antibody (YA3322)
    Immunohistochemical analysis of paraffin-embedded human lung cancer using MHC Class I antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P83577, 1/100) for 1 hour at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
  • Experimental Validation Results for MHC Class I Antibody (YA3322)
    Immunohistochemical analysis of paraffin-embedded human liver cancer using MHC Class I antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P83577, 1/100) for 1 hour at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
  • Experimental Validation Results for MHC Class I Antibody (YA3322)
    Immunohistochemical analysis of paraffin-embedded human cervical cancer using MHC Class I antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P83577, 1/100) for 1 hour at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
  • Experimental Validation Results for MHC Class I Antibody (YA3322)
    Immunohistochemical analysis of paraffin-embedded human ovarian cancer using MHC Class I antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P83577, 1/100) for 1 hour at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
  • Experimental Validation Results for MHC Class I Antibody (YA3322)
    Immunohistochemical analysis of paraffin-embedded human kidney using MHC Class I antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P83577, 1/100) for 1 hour at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
  • Experimental Validation Results for MHC Class I Antibody (YA3322)
    Immunohistochemical analysis of paraffin-embedded human renal cancer using MHC Class I antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P83577, 1/100) for 1 hour at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.

Background

  • Function

    MHC Class I is an Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-A-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells. May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity. Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells. Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome or via endopeptidase IDE/insulin-degrading enzyme. Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9; Allele A*01:01: Presents a restricted peptide repertoire including viral epitopes derived from IAV NP/nucleoprotein (CTELKLSDY), IAV PB1/polymerase basic protein 1 (VSDGGPNLY), HAdV-11 capsid L3/hexon protein (LTDLGQNLLY), SARS-CoV-2 3a/ORF3a (FTSDYYQLY) as well as tumor peptide antigens including MAGE1 (EADPTGHSY), MAGEA3 (EVDPIGHLY) and WT1 (TSEKRPFMCAY), all having in common a canonical motif with a negatively charged Asp or Glu residue at position 3 and a Tyr anchor residue at the C-terminus. A number of HLA-A*01:01-restricted peptides carry a post-translational modification with oxidation and N-terminal acetylation being the most frequent. Fails to present highly immunogenic peptides from the EBV latent antigens; Allele A*02:01: A major allele in human populations, presents immunodominant viral epitopes derived from IAV M/matrix protein 1 (GILGFVFTL), HIV-1 env (TLTSCNTSV), HIV-1 gag-pol (ILKEPVHGV), HTLV-1 Tax (LLFGYPVYV), HBV C/core antigen (FLPSDFFPS), HCMV UL83/pp65 (NLVPMVATV) as well as tumor peptide antigens including MAGEA4 (GVYDGREHTV), WT1 (RMFPNAPYL) and CTAG1A/NY-ESO-1 (SLLMWITQC), all having in common hydrophobic amino acids at position 2 and at the C-terminal anchors; Allele A*03:01: Presents viral epitopes derived from IAV NP (ILRGSVAHK), HIV-1 nef (QVPLRPMTYK), HIV-1 gag-pol (AIFQSSMTK), SARS-CoV-2 N/nucleoprotein (KTFPPTEPK) as well as tumor peptide antigens including PMEL (LIYRRRLMK), NODAL (HAYIQSLLK), TRP-2 (RMYNMVPFF), all having in common hydrophobic amino acids at position 2 and Lys or Arg anchor residues at the C-terminus. May also display spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein; Allele A*11:01: Presents several immunodominant epitopes derived from HIV-1 gag-pol and HHV-4 EBNA4, containing the peptide motif with Val, Ile, Thr, Leu, Tyr or Phe at position 2 and Lys anchor residue at the C-terminus. Important in the control of HIV-1, EBV and HBV infections. Presents an immunodominant epitope derived from SARS-CoV-2 N/nucleoprotein (KTFPPTEPK); Allele A*23:01: Interacts with natural killer (NK) cell receptor KIR3DL1 and may contribute to functional maturation of NK cells and self-nonself discrimination during innate immune response; Allele A*24:02: Presents viral epitopes derived from HIV-1 nef (RYPLTFGWCF), EBV lytic- and latent-cycle antigens BRLF1 (TYPVLEEMF), BMLF1 (DYNFVKQLF) and LMP2 (IYVLVMLVL), SARS-CoV nucleocapsid/N (QFKDNVILL), as well as tumor peptide antigens including PRAME (LYVDSLFFL), all sharing a common signature motif, namely an aromatic residue Tyr or Phe at position 2 and a nonhydrophobic anchor residue Phe, Leu or Iso at the C-terminus. Interacts with natural killer (NK) cell receptor KIR3DL1 and may contribute to functional maturation of NK cells and self-nonself discrimination during innate immune response; Allele A*26:01: Presents several epitopes derived from HIV-1 gag-pol (EVIPMFSAL, ETKLGKAGY) and env (LVSDGGPNLY), carrying as anchor residues preferentially Glu at position 1, Val or Thr at position 2 and Tyr at the C-terminus; Allele A*29:02: Presents peptides having a common motif, namely a Glu residue at position 2 and Tyr or Leu anchor residues at the C-terminus; Allele A*32:01: Interacts with natural killer (NK) cell receptor KIR3DL1 and may contribute to functional maturation of NK cells and self-nonself discrimination during innate immune response; Allele A*68:01: Presents viral epitopes derived from IAV NP (KTGGPIYKR) and HIV-1 tat (ITKGLGISYGR), having a common signature motif namely, Val or Thr at position 2 and positively charged residues Arg or Lys at the C-terminal anchor; Allele A*74:01: Presents immunodominant HIV-1 epitopes derived from gag-pol (GQMVHQAISPR, QIYPGIKVR) and rev (RQIHSISER), carrying an aliphatic residue at position 2 and Arg anchor residue at the C-terminus. May contribute to viral load control in chronic HIV-1 infection[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36].

  • Subcellular Localization

    Cell membrane; Single-pass type I membrane protein; Endoplasmic reticulum membrane; Single-pass type I membrane protein

  • Expression


    Tissue_specificity:general expression

    Induction:Up-regulated by IFNG, and pro-inflammatory cytokines IL1B and TNF

  • Isoforms & Post-Translational Modification

    P04439 has 2 isomers: P04439-1: 40841 Da (predicted); P04439-2: 41394 Da (predicted).
    (Microbial infection) Polyubiquitinated in a post ER compartment by interaction with human herpesvirus 8 MIR1 protein. This targets the protein for rapid degradation via the ubiquitin system;N-linked glycosylation at Asn-110

  • Subunit

    Heterotrimer that consists of an alpha chain HLA-A, a beta chain B2M and a peptide (peptide-HLA-A-B2M) (PubMed:11502003, PubMed:18275829, PubMed:19177349, PubMed:19542454, PubMed:21943705, PubMed:22245737, PubMed:24395804, PubMed:26758806, PubMed:28250417, PubMed:7504010, PubMed:7506728, PubMed:7679507, PubMed:7694806, PubMed:7935798, PubMed:8805302, PubMed:8906788, PubMed:9177355). Early in biogenesis, HLA-A-B2M dimer interacts with the components of the peptide-loading complex composed of TAPBP, TAP1-TAP2, TAPBPL, PDIA3/ERP57 and CALR (PubMed:21263072). Interacts with TAP1-TAP2 transporter via TAPBP; this interaction is obligatory for the loading of peptide epitopes delivered to the ER by TAP1-TAP2 transporter (PubMed:21263072, PubMed:8630735, PubMed:8805302). Interacts with TAPBPL; TAPBPL binds peptide-free HLA-A-B2M complexes or those loaded with low affinity peptides, likely facilitating peptide exchange for higher affinity peptides (PubMed:26869717, PubMed:35725941). Only optimally assembled peptide-HLA-B2M trimer translocates to the surface of antigen-presenting cells, where it interacts with TCR and CD8 coreceptor on the surface of T cells. HLA-A (via polymorphic alpha-1 and alpha-2 domains) interacts with antigen-specific TCR (via CDR3 domains) (PubMed:12796775, PubMed:18275829, PubMed:22245737). One HLA-A molecule (mainly via nonpolymorphic alpha-3 domain) interacts with one CD8A homodimer (via CDR-like loop); this interaction ensures peptide-HLA-A-B2M recognition by CD8-positive T cells only (PubMed:2784196, PubMed:9177355). Alleles A*23:01; A*24:02 and A*32:01 interact (via Bw4 motif) with KIR3DL1 on NK cells; this interaction is direct

  • SwissProt ID

    P04439

  • Gene ID
  • Synonyms

    Aw-68; HLA class I histocompatibility antigen; A-28 alpha chain; MHC class I antigen A*68; HLA-A; MHC class I antigen HLA A heavy chain

  • Research Field

    Immunology

References

[1]. Fukada K, et al. HLA-A*1101-restricted cytotoxic T lymphocyte recognition of HIV-1 Pol protein. AIDS. 1999 Jul 30;13(11):1413-4. [Content Brief]

[2]. Nagata Y, et al. Differential presentation of a soluble exogenous tumor antigen, NY-ESO-1, by distinct human dendritic cell populations. Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10629-34. [Content Brief]

[3]. Kuzushima K, et al. Tetramer-assisted identification and characterization of epitopes recognized by HLA A*2402-restricted Epstein-Barr virus-specific CD8+ T cells. Blood. 2003 Feb 15;101(4):1460-8. [Content Brief]

[4]. Traversari C, et al. A nonapeptide encoded by human gene MAGE-1 is recognized on HLA-A1 by cytolytic T lymphocytes directed against tumor antigen MZ2-E. J Exp Med. 1992 Nov 1;176(5):1453-7. [Content Brief]

[5]. Satoh M, et al. Identification and characterization of HIV-1-specific CD8+ T cell epitopes presented by HLA-A*2601. Vaccine. 2005 May 31;23(29):3783-90. [Content Brief]

[6]. Asemissen AM, et al. Identification of a highly immunogenic HLA-A*01-binding T cell epitope of WT1. Clin Cancer Res. 2006 Dec 15;12(24):7476-82. [Content Brief]

[7]. Hadrup SR, et al. Parallel detection of antigen-specific T-cell responses by multidimensional encoding of MHC multimers. Nat Methods. 2009 Jul;6(7):520-6. [Content Brief]

[8]. Matthews PC, et al. HLA-A*7401-mediated control of HIV viremia is independent of its linkage disequilibrium with HLA-B*5703. J Immunol. 2011 May 15;186(10):5675-86. [Content Brief]

[9]. Shimizu A, et al. Structure of TCR and antigen complexes at an immunodominant CTL epitope in HIV-1 infection. Sci Rep. 2013 Nov 6;3:3097. [Content Brief]

[10]. Quiñones-Parra S, et al. Preexisting CD8+ T-cell immunity to the H7N9 influenza A virus varies across ethnicities. Proc Natl Acad Sci U S A. 2014 Jan 21;111(3):1049-54. [Content Brief]

[11]. Jelachich ML, et al. Analysis of the molecular basis of HLA-A3 recognition by cytotoxic T cells using defined mutants of the HLA-A3 molecule. J Immunol. 1988 Aug 15;141(4):1108-13. [Content Brief]

[12]. Salter RD, et al. Polymorphism in the alpha 3 domain of HLA-A molecules affects binding to CD8. Nature. 1989 Mar 23;338(6213):345-7. [Content Brief]

[13]. Song I, et al. Broad TCR repertoire and diverse structural solutions for recognition of an immunodominant CD8(+) T cell epitope. Nat Struct Mol Biol. 2017 Apr;24(4):395-406. [Content Brief]

[14]. DiBrino M, et al. HLA-A1 and HLA-A3 T cell epitopes derived from influenza virus proteins predicted from peptide binding motifs. J Immunol. 1993 Dec 1;151(11):5930-5. [Content Brief]

[15]. Madden DR, et al. The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell. 1993 Nov 19;75(4):693-708. [Content Brief]

[16]. Kawakami Y, et al. Identification of new melanoma epitopes on melanosomal proteins recognized by tumor infiltrating T lymphocytes restricted by HLA-A1, -A2, and -A3 alleles. J Immunol. 1998 Dec 15;161(12):6985-92. [Content Brief]

[17]. Giam K, et al. A comprehensive analysis of peptides presented by HLA-A1. Tissue Antigens. 2015 Jun;85(6):492-6. [Content Brief]

[18]. DiBrino M, et al. Endogenous peptides with distinct amino acid anchor residue motifs bind to HLA-A1 and HLA-B8. J Immunol. 1994 Jan 15;152(2):620-31. [Content Brief]

[19]. DiBrino M, et al. Endogenous peptides bound to HLA-A3 possess a specific combination of anchor residues that permit identification of potential antigenic peptides. Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1508-12. [Content Brief]

[20]. Stewart-Jones GB, et al. A structural basis for immunodominant human T cell receptor recognition. Nat Immunol. 2003 Jul;4(7):657-63. [Content Brief]

[21]. Ishizuka J, et al. The structural dynamics and energetics of an immunodominant T cell receptor are programmed by its Vbeta domain. Immunity. 2008 Feb;28(2):171-82. [Content Brief]

[22]. Gras S, et al. Structural bases for the affinity-driven selection of a public TCR against a dominant human cytomegalovirus epitope. J Immunol. 2009 Jul 1;183(1):430-7. [Content Brief]

[23]. Robek MD, et al. Role of immunoproteasome catalytic subunits in the immune response to hepatitis B virus. J Virol. 2007 Jan;81(2):483-91. [Content Brief]

[24]. Parmentier N, et al. Production of an antigenic peptide by insulin-degrading enzyme. Nat Immunol. 2010 May;11(5):449-54. [Content Brief]

[25]. Tripathi SC, et al. Immunoproteasome deficiency is a feature of non-small cell lung cancer with a mesenchymal phenotype and is associated with a poor outcome. Proc Natl Acad Sci U S A. 2016 Mar 15;113(11):E1555-64. [Content Brief]

[26]. Ebstein F, et al. Proteasomes generate spliced epitopes by two different mechanisms and as efficiently as non-spliced epitopes. Sci Rep. 2016 Apr 6;6:24032. [Content Brief]

[27]. Kumar P, et al. Conformational changes within the HLA-A1:MAGE-A1 complex induced by binding of a recombinant antibody fragment with TCR-like specificity. Protein Sci. 2009 Jan;18(1):37-49. [Content Brief]

[28]. Raman MC, et al. Direct molecular mimicry enables off-target cardiovascular toxicity by an enhanced affinity TCR designed for cancer immunotherapy. Sci Rep. 2016 Jan 13;6:18851. [Content Brief]

[29]. Keib A, et al. Measuring Antiviral Capacity of T Cell Responses to Adenovirus. J Immunol. 2019 Jan 15;202(2):618-624. [Content Brief]

[30]. Peng Y, et al. Broad and strong memory CD4(+) and CD8(+) T cells induced by SARS-CoV-2 in UK convalescent individuals following COVID-19. Nat Immunol. 2020 Nov;21(11):1336-1345. [Content Brief]

[31]. Brennan RM, et al. A mechanism for the HLA-A*01-associated risk for EBV+ Hodgkin lymphoma and infectious mononucleosis. Blood. 2008 Sep 15;112(6):2589-90. [Content Brief]

[32]. Zhang S, et al. Structural basis of cross-allele presentation by HLA-A*0301 and HLA-A*1101 revealed by two HIV-derived peptide complexes. Mol Immunol. 2011 Oct;49(1-2):395-401. [Content Brief]

[33]. Liu J, et al. Novel immunodominant peptide presentation strategy: a featured HLA-A*2402-restricted cytotoxic T-lymphocyte epitope stabilized by intrachain hydrogen bonds from severe acute respiratory syndrome coronavirus nucleocapsid protein. J Virol. 2010 Nov;84(22):11849-57. [Content Brief]

[34]. Ikeda H, et al. Characterization of an antigen that is recognized on a melanoma showing partial HLA loss by CTL expressing an NK inhibitory receptor. Immunity. 1997 Feb;6(2):199-208. [Content Brief]

[35]. Thananchai H, et al. Cutting Edge: Allele-specific and peptide-dependent interactions between KIR3DL1 and HLA-A and HLA-B. J Immunol. 2007 Jan 1;178(1):33-7. [Content Brief]

[36]. Stern M, et al. Human leukocyte antigens A23, A24, and A32 but not A25 are ligands for KIR3DL1. Blood. 2008 Aug 1;112(3):708-10. [Content Brief]

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