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SEC22B antibody (SEC22 Vesicle Trafficking Protein Homolog B (S. Cerevisiae) (Gene/pseudogene))

Details for Product anti-SEC22B Antibody No. ABIN351372, Supplier: Log in to see
Antigen
  • 4930564D15Rik
  • AA517334
  • AI480645
  • C81333
  • ERS-24
  • ers-24
  • Ers24
  • sec22b
  • SEC22L1
  • Sec22l1
  • sec22l1
Reactivity
Human, Rat (Rattus), Mouse (Murine)
48
11
11
Host
Sheep
33
13
2
Clonality
Polyclonal
Conjugate
This SEC22B antibody is un-conjugated
3
3
3
3
3
3
Application
Immunohistochemistry (IHC), Western Blotting (WB)
46
30
19
7
3
2
1
Supplier
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Immunogen A synthetic peptide from human SEC22b conjugated to an immunogenic carrier protein was used as the antigen.
Isotype IgG
Specificity Specific for SEC22B.
Alternative Name SEC22B (SEC22B Antibody Abstract)
Background The protein encoded by this gene is a member of the SEC22 family of vesicle trafficking proteins. It seems to complex with SNARE and it is thought to play a role in the ER-Golgi protein trafficking. This protein has strong similarity to Mus musculus and Cricetulus griseus proteins. There is evidence for use of multiple polyadenylation sites for the transcript.
Function: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER.
Subunit: Component of two distinct SNARE complexes consisting of STX5,GOSR2/BOS1, BET1 and SEC22B or STX18, USE1L, BNIP1/SEC20L and SEC22B. YKT6 can probably replace SEC22B in either complex.
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane, Single-pass type IV membrane protein. Golgi apparatus membrane, Single-pass type IV membrane protein. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Also known as: SEC22 vesicle-trafficking protein homolog B, SEC22 vesicle-trafficking protein-like 1, ERS24, ERS-24, Vesicle-trafficking protein SEC22b, SEC22L1, SEC22B.
Application Notes A concentration of 10-50 µg/ml is recommended.
The optimal concentration should be determined by the end user.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in 100 µL of sterile water. Centrifuge to remove any insoluble material.
Handling Advice Avoid freeze and thaw cycles.
Storage 4 °C/-20 °C
Storage Comment Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.
Expiry Date 12 months
Background publications Matsuoka, Ballif, Smogorzewska, McDonald, Hurov, Luo, Bakalarski, Zhao, Solimini, Lerenthal, Shiloh, Gygi, Elledge: "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." in: Science (New York, N.Y.), Vol. 316, Issue 5828, pp. 1160-6, 2007

Villén, Beausoleil, Gerber, Gygi: "Large-scale phosphorylation analysis of mouse liver." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, Issue 5, pp. 1488-93, 2007

Chi, Valencia, Hu, Watabe, Yamaguchi, Mangini, Huang, Canfield, Cheng, Yang, Abe, Yamagishi, Shabanowitz, Hearing, Wu, Appella, Hunt: "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." in: Journal of proteome research, Vol. 5, Issue 11, pp. 3135-44, 2006

Carninci, Kasukawa, Katayama, Gough, Frith, Maeda, Oyama, Ravasi, Lenhard, Wells, Kodzius, Shimokawa, Bajic, Brenner, Batalov, Forrest, Zavolan, Davis, Wilming, Aidinis, Allen, Ambesi-Impiombato et al.: "The transcriptional landscape of the mammalian genome. ..." in: Science (New York, N.Y.), Vol. 309, Issue 5740, pp. 1559-63, 2005

Nakajima, Hirose, Taniguchi, Kurashina, Arasaki, Nagahama, Tani, Yamamoto, Tagaya: "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusion." in: The EMBO journal, Vol. 23, Issue 16, pp. 3216-26, 2004

Volchuk, Ravazzola, Perrelet, Eng, Di Liberto, Varlamov, Fukasawa, Engel, Soellner, Rothman, Orci: "Countercurrent distribution of two distinct SNARE complexes mediating transport within the Golgi stack." in: Molecular biology of the cell, Vol. 15, Issue 4, pp. 1506-18, 2004

Xu, Joglekar, Williams, Hay: "Subunit structure of a mammalian ER/Golgi SNARE complex." in: The Journal of biological chemistry, Vol. 275, Issue 50, pp. 39631-9, 2001

Gonzalez, Weis, Scheller: "A novel snare N-terminal domain revealed by the crystal structure of Sec22b." in: The Journal of biological chemistry, Vol. 276, Issue 26, pp. 24203-11, 2001

Mao, Fu, Wu, Zhang, Zhou, Kan, Huang, He, Gu, Han, Shen, Gu, Yu, Xu, Wang, Chen, Chen: "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 95, Issue 14, pp. 8175-80, 1998

Hay, Chao, Kuo, Scheller: "Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells." in: Cell, Vol. 89, Issue 1, pp. 149-58, 1997