Trim5a (Intermediate Domain – 1) Blocking Peptide

Trim5a (Intermediate Domain – 1) Blocking Peptide

Product No.: T337

[product_table name="All Top" skus="T337"]

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Target
TRIM5α
Product Type
Blocking Peptide
Alternate Names
Tripartite-Motif Containing 5α
Applications
IHC FF
,
IHC FFPE
,
N
,
WB

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Select Product Size
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Antibody Details

Product Details

Reactive Species
Human
Product Concentration
0.2 mg/ml
Amino Acid Location
15 Amino acids from towards the C-terminus of human TRIM5α.
Formulation
This peptide is formulated in PBS pH 7.2 (0.01 M Sodium Phosphate, 0.13 M NaCl) containing 0.1% bovine serum albumin and 0.02% sodium azide.
Storage and Handling
Store this peptide in working aliquots at -20°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles.
Country of Origin
USA
Shipping
Next Day Ambient
Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.

Description

Background
TRIM5α peptide is applicable as a control peptide for blocking antibody binding in Western blotting.

References & Citations

1. Fanning AS and Anderson JM. Protein modules as organizers of membrane structure.Curr. Opin. Cell Biol. 1999; 11:432-9. 2. Gaide O, Martinon F, Michau O, et al. Carma1, 1 CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-κ B activation. FEBS Lett. 2001; 496:121-7. 3. Bertin J, Wang L, Guo Y, et al. CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-κ B. J. Biol. Chem. 2001; 276:11877-82. 4. McAllister-Lucas LM, Inohara N, Lucas PC, et al. Bimp1, a MAGUK family member linking protein kinase C activation to Bcl10-mediated NF-κB induction. J. Biol. Chem. 2001; 276:30589-97.
IHC FF
IHC FFPE
N
General Western Blot Protocol

Certificate of Analysis

Disclaimer AlertProducts are for research use only. Not for use in diagnostic or therapeutic procedures.