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TCP-1 α monoclonal antibody (23c)

ADI-CTA-123

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TCP-1alpha is a 60 kDa subunit of a cytosolic hetero-oligomer chaperone that is known to be involved in the folding of Actin and Tubulin. This protein is a member of the Chaperonin family, which includes E. coli GroEL, the mitochondrial Heat-shock protein Hsp60, the plastid Rubisco-subunit-binding protein, and the archaebacterial protein TF55. These Chaperonins assist the folding of proteins upon ATP hydrolysis.

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This antibody is covered by our Worry-Free Guarantee.

TCP-1 α monoclonal antibody (23c) Western blot — Western blot analysis of TCP-1a: Lane 1: MW marker, Lane 2: Hsp60 Recombinant Human Protein, Lane 3: 3T3 Heat Shocked, Lane 4: PC-12 Heat Shocked.

Product Details

Alternative Name	CCT, p63, Tric, T-complex 1
Application	ICC, IHC, IP, WB
Application Notes	Detects a band of ~60kDa by Western blot.
Clone	23c
Formulation	Liquid. In PBS containing 50% glycerol and 0.09% sodium azide.
GenBank ID	D90344
Host	Rat
Immunogen	Recombinant mouse TCP-1α (C-terminal fragment).
Isotype	IgG2c
Purity Detail	Protein G affinity purified.
Recommendation Dilutions/Conditions	Western Blot (1:1,000, colorimetric)Suggested dilutions/conditions may not be available for all applications.Optimal conditions must be determined individually for each application.
Source	Purified from mouse ascites.
Species Reactivity	Chicken, Dog, Hamster, Human, Mouse, Plant, Rabbit, Rat, Sheep
UniProt ID	P11983
Worry-free Guarantee	This antibody is covered by our Worry-Free Guarantee.

Handling & Storage

Handling	Avoid freeze/thaw cycles.
Long Term Storage	-20°C
Shipping	Blue Ice

Regulatory Status	RUO – Research Use Only

The TRiC chaperonin controls reovirus replication through outer-capsid folding.: Knowlton, J. J., Fernández de Castro, I., et al.; Nat. Microbiol. 3, 481 (2018), Application(s): WB, Abstract
The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol: Spillman, N. J., Beck, J. R., et al.; Cell. Microbiol. 19, (2017), Abstract
Association of Simian Virus 40 Vp1 with 70-Kilodalton Heat ShockProteins and Viral Tumor Antigens: H. Kasamatsu, et al.; J. Virol. 83, 37 (2008), Application(s): WB, IP using monkey cell lysates, Abstract
Identification of a host protein essential for assembly of immature HIV-1 capsids: J.R. Lingappa, et al.; Nature 415, 88 (2002), Application(s): IP using plant (wheat) samples, Abstract
The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking: J. Frydman, et al.; J. Cell Biol. 149, 591 (2000), Application(s): IP using rabbit samples, Abstract
A 102 kDa subunit of a Golgi-associated particle has homology to beta subunits of trimeric G proteins: K.R. Willison, et al.; EMBO J. 12, 2847 (1993), Application(s): WB, ICC using human, mouse, rat, & chicken samples, Abstract
T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol: K. Willison, et al.; Nature 358, 249 (1992), Application(s): ICC using human samples, Abstract