BAP1 Antibody [L1A7] | Primary Antibodies

Application: Reactivity: Rat, Mouse, Human

Lane 1: Hela, Lane 2: PC3, Lane 3: A549, Lane 4: HepG2

Usage Information

Dilution
WB1:1000 IHC1:100 FCM1:60

Application
WB, IHC, FCM

Reactivity
Rat, Mouse, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
80 kDa 100 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human colon carcinoma; Human lung carcinoma tissue; Rat cerebrum tissue; Mouse cerebrum tissue; HeLa cells; PC-3 cells; A375 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
BAP1 Antibody [L1A7] detects endogenous levels of total BAP1 protein.

Clone
L1A7

Synonym(s)
KIAA0272; hucep-6; BAP1; Ubiquitin carboxyl-terminal hydrolase BAP1; BRCA1-associated protein 1; Cerebral protein 6

Background
BRCA1-associated protein 1 (BAP1) is a 729-amino-acid nuclear-cytoplasmic deubiquitinating enzyme (DUB) from the UCH family and acts as a potent tumor suppressor encoded by the BAP1 gene. It primarily localizes to the nucleus via C-terminal signals (amino acids 656–661 and 717–722) to regulate chromatin dynamics, DNA repair, and gene expression. Germline or somatic mutations in BAP1 underlie BAP1 tumor predisposition syndrome (BAP1-TPDS) and are implicated in cancers such as uveal melanoma, mesothelioma, renal cell carcinoma, and cutaneous melanomas. BAP1 contains an N-terminal catalytic UCH domain (amino acids 1–250; key residues Cys91, His169, Asp184 for deubiquitination), a ubiquitin-like (UBL) domain, and C-terminal binding motifs for ASXL1/2 (amino acids 635–693, forming the PR-DUB complex), HCF-1 (amino acids 365–385), BARD1 (amino acids 182–365), and BRCA1 (amino acids 596–721). These enable multiprotein interactions but BAP1 does not directly deubiquitinate BRCA1/BARD1; instead, it inhibits their E3 ligase activity through dimerization blockade. Functionally, BAP1 deubiquitinates H2AK119 (via the PR-DUB complex) to repress transcription (e.g., SLC7A11, promoting ferroptosis), stabilizes HCF-1 for cell cycle control, and acts on IP3R3 (in the cytoplasm) to promote Ca²⁺-dependent apoptosis. It also supports BRCA1/BARD1-independent DNA repair, the unfolded protein response under stress, metabolic regulation (NADPH balance, disulfidptosis suppression), and cellular differentiation. Biallelic inactivation of BAP1 in tumors disrupts these functions, resulting in genomic instability, immune evasion, and cancer progression.

Background

BRCA1-associated protein 1 (BAP1) is a 729-amino-acid nuclear-cytoplasmic deubiquitinating enzyme (DUB) from the UCH family and acts as a potent tumor suppressor encoded by the BAP1 gene. It primarily localizes to the nucleus via C-terminal signals (amino acids 656–661 and 717–722) to regulate chromatin dynamics, DNA repair, and gene expression. Germline or somatic mutations in BAP1 underlie BAP1 tumor predisposition syndrome (BAP1-TPDS) and are implicated in cancers such as uveal melanoma, mesothelioma, renal cell carcinoma, and cutaneous melanomas. BAP1 contains an N-terminal catalytic UCH domain (amino acids 1–250; key residues Cys91, His169, Asp184 for deubiquitination), a ubiquitin-like (UBL) domain, and C-terminal binding motifs for ASXL1/2 (amino acids 635–693, forming the PR-DUB complex), HCF-1 (amino acids 365–385), BARD1 (amino acids 182–365), and BRCA1 (amino acids 596–721). These enable multiprotein interactions but BAP1 does not directly deubiquitinate BRCA1/BARD1; instead, it inhibits their E3 ligase activity through dimerization blockade. Functionally, BAP1 deubiquitinates H2AK119 (via the PR-DUB complex) to repress transcription (e.g., SLC7A11, promoting ferroptosis), stabilizes HCF-1 for cell cycle control, and acts on IP3R3 (in the cytoplasm) to promote Ca²⁺-dependent apoptosis. It also supports BRCA1/BARD1-independent DNA repair, the unfolded protein response under stress, metabolic regulation (NADPH balance, disulfidptosis suppression), and cellular differentiation. Biallelic inactivation of BAP1 in tumors disrupts these functions, resulting in genomic instability, immune evasion, and cancer progression.

References
https://pubmed.ncbi.nlm.nih.gov/37246324/ https://pubmed.ncbi.nlm.nih.gov/39842618/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%