You Searched For: Antibodies

Catalog Number: (RL710-1602)

Supplier: Rockland Immunochemical

Description: This product has been assayed against 1.0 µg of Mouse IgG in a standard capture ELISA using Peroxidase Conjugated Streptavidin and ABTS (2,2’-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid])

Catalog Number: (RL709-1611)

Supplier: Rockland Immunochemical

Description: This product has been assayed against 1.0 µg of Human IgG in a standard capture ELISA using Peroxidase Conjugated Streptavidin and ABTS (2,2’-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid])

Supplier: Enzo Life Sciences

Description: Grp75 (Glucose regulated 75 kDa protein) is a member of the Hsp70 family. It is localized in the mitochondrial matrix, where, in concert with Hsp60, is thought to participate in the re-folding of proteins translocated into this organelle. Like its E. coli homolog DnaK, Grp75 possesses a cation-dependent ATPase activity thought to be central to its function as a chaperone.

Supplier: Enzo Life Sciences

Description: Fas/APO-1/CD95 is a 36 kDa cell surface type I-membrane glycoprotein with an apparent molecular weight of 44 kDa on SDS-PAGE.  Fas belongs to the tumor necrosis factor receptor (TNFR) family, which includes TNFR1, TNFR2, CD27, CD30 and CD40.  Binding of Fas-ligand (FasL) to Fas or crosslinking of Fas by anti-Fas monoclonal antibodies leads to apoptosis of Fas expressing cells.  Both Fas and TNFR contain a 70 amino acid cytoplasmic “death domain” responsible for transmitting signals for apoptosis.  Apoptosis induced by Fas-Fas ligand interaction is inhibited by a number of cytosolic factors such as the ICE/CED3 family inhibitor CrmA, and the short and long forms of FLIP. Insertion of an early transposable element in intron 2 of the Fas gene, as in the mouse lpr mutations, causes lymphoproliferation and autoimmunity in mutant mice, suggesting the involvement of Fas in clonal deletion of autoreactive T cells.

SDS

Supplier: Enzo Life Sciences

Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Catalog Number: (95043-816)

Supplier: Enzo Life Sciences

Description: Hsp25 is a member of the family of small heat shock proteins (sHsps), an evolutionarily conserved family of stress proteins which exhibit moleclular weights between 14-45 kDa. The sHsps are related to the alpha-crystallins, and generally exist as large oligomeric complexes that serve to stabilize and assist in refolding of denatured proteins. Hsp25 is highly homologous to the human Hsp27, and its expression is seen in many species, including mouse, rat, bovine, canine, and hamster cells.

SDS

Catalog Number: (RL605-746-125)

Supplier: Rockland Immunochemical

Description: Anti-IgG Donkey Polyclonal Antibody (DyLight® 405)

Catalog Number: (RL600-446-381)

Supplier: Rockland Immunochemical

Description: Primary Rabbit Anti-MYC EPITOPE TAG Reacts with Pan

Catalog Number: (RL603143126)

Supplier: Rockland Immunochemical

Description: Anti-IgG Goat Polyclonal Antibody (DyLight® 649)

Catalog Number: (RL613-4202)

Supplier: Rockland Immunochemical

Description: Secondary Rabbit Anti-IgG (H&L) Reacts with Sheep (Ovine)

SDS

Catalog Number: (RL612-6502)

Supplier: Rockland Immunochemical

Description: This product has been assayed against 1.0 µg of Rat IgG in a standard capture ELISA using pNPP p-nitrophenyl phosphate as a substrate for 30 minutes at room temperature.

Catalog Number: (RL611-644-122)

Supplier: Rockland Immunochemical

Description: Anti-IgG Sheep Polyclonal Antibody (DyLight® 680)

Catalog Number: (RL612-4504)

Supplier: Rockland Immunochemical

Description: This product has been assayed against 1.0 µg of Rat IgG in a standard capture ELISA using pNPP p-nitrophenyl phosphate as a substrate for 30 minutes at room temperature.

SDS

Catalog Number: (RL612-1902)

Supplier: Rockland Immunochemical

Description: Secondary Goat Anti-IgG (H&L) Reacts with Rat

SDS

Supplier: Enzo Life Sciences

Description: The caspases are a family of cysteine proteases that cleave after certain aspartate residues, and are primarily recognized as mediators of apoptosis. caspases are synthesized as inactive zymogens that can be cleaved to form active enzymes following the induction of apoptosis by stress or death receptors. Initiator caspases (e.g. caspase-8 and -10) are activated by dimerization of the zymogen on a dedicated adaptor protein. These activated initiator caspases in-turn cleave downstream effector or executioner caspases (e.g. caspase-3, -6, and -7) in a cascade-like manner, which cleave key cellular proteins that lead to the morphological changes associated with apoptotic cell death.

Supplier: Enzo Life Sciences

Description: The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.