MCL1 Antibody (YA5869)
(Synonyms: MCL1; BCL2L3; Induced myeloid leukemia cell differentiation protein Mcl-1; Bcl-2-like protein 3; Bcl2-L-3; Bcl-2-related protein EAT/mcl1; mcl1/EAT)
Based on 1 Customer Validation
MCL1 Antibody (YA5869) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to MCL1.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF, IP, ELISA
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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IP
IP: Immunoprecipitation
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|---|---|---|---|---|---|
| Dilution Ratio | 1:200-1:1000 | 1:2000-1:10000 | 1:200-1:1000 | 1:5000-1:20000 | 1:50-1:200 |
Product Details
MCL1 Antibody (YA5869) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to MCL1.
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Host Rabbit
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 37 kDa
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.
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Calculated Molecular Weight Predicted band size: 37 kDa
Protein A
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Mcl-1 (myeloid cell leukemia-1) is a critical anti-apoptotic member of the BCL-2 protein family that preserves mitochondrial integrity by restraining the pro-apoptotic effectors BAK and BAX and preventing mitochondrial outer membrane permeabilization (MOMP) [1][2]. Mechanistically, Mcl-1 contains a hydrophobic BH3-binding groove that sequesters pro-apoptotic proteins and suppresses stress-induced apoptosis, thereby maintaining cell survival under physiological and pathological conditions[1][3]. Within the intrinsic apoptotic pathway, BH3-only proteins including NOXA, BIM, PUMA, and BID antagonize anti-apoptotic BCL-2 family members, and NOXA displays notable selectivity toward Mcl-1, promoting apoptotic signaling through Mcl-1 neutralization and degradation[4][5][6]. In cancer models, Mcl-1 overexpression contributes to tumor progression, chemoresistance, and disease relapse, highlighting its role as a major survival factor in malignant cells[7][8]. Compared with related anti-apoptotic isoforms such as BCL-2 and BCL-xL, Mcl-1 exhibits distinct binding preferences and plays a particularly important role in restraining BAK-dependent apoptosis, indicating non-redundant functions within the BCL-2 family network[9][10]. For experimental applications, selective Mcl-1 inhibitors and BH3 mimetics, including MCL-1 SAHB and S63845, disrupt Mcl-1-BAK interactions and induce apoptosis in MCL-1-dependent cancer cells, providing valuable tools for mechanistic studies and therapeutic target validation[11][12].
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Subcellular Localization
Membrane; Single-pass membrane protein; Cytoplasm; Mitochondrion; Nucleus, nucleoplasm
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Expression
Induction:Expression increases early during phorbol ester-induced differentiation along the monocyte/macrophage pathway in myeloid leukemia cell line ML-1. Rapidly up-regulated by CSF2 in ML-1 cells. Up-regulated by heat shock-induced differentiation. Expression increases early during retinoic acid-induced differentiation -
Isoforms & Post-Translational Modification
Q07820 has 2 isomers: Q07820-1: 37337 Da (predicted); Q07820-2: 28662 Da (predicted).
Cleaved by CASP3 during apoptosis. In intact cells cleavage occurs preferentially after Asp-127, yielding a pro-apoptotic 28 kDa C-terminal fragment;Rapidly degraded in the absence of phosphorylation on Thr-163 in the PEST region;Phosphorylated on Ser-159, by GSK3, in response to IL3/interleukin-3 withdrawal. Phosphorylation at Ser-159 induces ubiquitination and proteasomal degradation, abrogating the anti-apoptotic activity. Treatment with taxol or okadaic acid induces phosphorylation on additional sites;Ubiquitinated. Ubiquitination is induced by phosphorylation at Ser-159 (PubMed:16543145). Deubiquitinated by USP20; leading to increased stability (PubMed:35063767) -
Subunit
Interacts with HIF3A (via C-terminus domain) (By similarity). Interacts with BAD, BOK, BIK and BMF (By similarity). Interacts with PMAIP1 (PubMed:17389404). Interacts with BBC3 (By similarity). Isoform 1 interacts with BAX, BAK1 and TPT1 (PubMed:10837489, PubMed:12149273, PubMed:15077116). Heterodimer of isoform 1 and isoform 2. Homodimers of isoform 1 or isoform 2 are not detected. Isoform 2 does not interact with pro-apoptotic BCL2-related proteins (PubMed:10837489). Interacts with RTL10/BOP (PubMed:23055042). Interacts with BCL2L11; may sequester BCL2L11 to prevent its pro-apoptotic activity (PubMed:10837489, PubMed:17389404, PubMed:20562877, PubMed:27013495). Interacts with GIMAP5 and HSPA8/HSC70; the interaction between HSPA8 and MCL1 is impaired in the absence of GIMAP5 (By similarity)
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SwissProt ID
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Synonyms
MCL1; BCL2L3; Induced myeloid leukemia cell differentiation protein Mcl-1; Bcl-2-like protein 3; Bcl2-L-3; Bcl-2-related protein EAT/mcl1; mcl1/EAT
Documentation
[1]. Chipuk JE, et al. How do BCL-2 proteins induce mitochondrial outer membrane permeabilization? Trends Cell Biol. 2008 Apr;18(4):157-64. [Content Brief]
[3]. Huang K, et al. BH3-only proteins target BCL-xL/MCL-1, not BAX/BAK, to initiate apoptosis. Cell Res. 2019 Nov;29(11):942-952. [Content Brief]
[9]. Zhai D, et al. Differential regulation of Bax and Bak by anti-apoptotic Bcl-2 family proteins Bcl-B and Mcl-1. J Biol Chem. 2008 Apr 11;283(15):9580-6. [Content Brief]
[10]. Willis SN, et al. Life in the balance: how BH3-only proteins induce apoptosis. Curr Opin Cell Biol. 2005 Dec;17(6):617-25. [Content Brief]
[11]. Stewart ML, et al. The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer. Nat Chem Biol. 2010 Aug;6(8):595-601. [Content Brief]
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