Septin 9 (SEPTIN9) Antibody

Product Graph
292.5€ (80 µl)

Por favor contáctenos para obtener información detallada sobre el precio y disponibilidad.

935106861
info@markelab.com
name
Septin 9 (SEPTIN9) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx032735
tested applications
ELISA, WB, IHC, FCM

Description

The maf oncogene was identified by structural analysis of the AS42 avian transforming retrovirus genome. The Maf family is divided into two subclasses, large Mafs (vMaf, cMaf, MafB and Nrl) and small Mafs (MafF, MafK, and MafG). Both subclasses contain leucinezipper motifs, which allow homodimerization as well as heterodimerization with a variety of other bZip transcription factors. Large Mafs also contain an acidic transactivation domain absent in the small Maf proteins. Although they do not possess inherent transactivation activity, small Maf proteins can act as positive regulators of transcription by targeting transcriptionally active dimerization partners to specific DNA regulatory elements. Conversely, small Mafs can act also as negative regulators of transcription by recruiting transcriptional repressors or by forming homodimers that can replace active dimers. Human MafF was isolated in a yeast one-hybrid system from a human myometrium cDNA library. Human MAFF encodes a 164 amino acids proten. Like other small MAFF proteins, it contains an extended leucine zipper structure and lacks an N-terminal transactivating domain. The three small Maf proteins have been implicated in a number of physiological processes, including development, differentiation, haematopoiesis and stress response. Interestingly, these three proteins regulate the stress response via different mechanisms.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Primary Antibodies
Immunogen Target
Septin 9 (SEPTIN9)
Host
Rabbit
Reactivity
Human
Recommended Dilution
WB: 1/1000, IHC-P: 1/50 - 1/100, FCM: 1/10 - 1/50. Not tested in IHC-F. Optimal dilutions/concentrations should be determined by the end user.
Clonality
Polyclonal
Conjugation
Unconjugated
Isotype
IgG
Purification
Purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, followed by dialysis against PBS.
Size 1
80 µl
Size 2
400 µl
Form
Liquid
Tested Applications
ELISA, WB, IHC, FCM
Buffer
PBS containing 0.09% sodium azide.
Availability
Shipped within 5-10 working days.
Storage
Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
Q9UHD8
NCBI Accession
NP_001106963.1, NP_001106964.1, NP_001106965.1, NP_001106966.1, NP_001106967.1, NP_001106968.1, NP_006631.2
Background
Antibody anti-SEPTIN9
Status
RUO

Descripción

Related Products

FNab07729

SEPTIN9 antibody

Filament-forming cytoskeletal GTPase(By similarity). May play a role in cytokinesis(Potential). May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri.

Ver Producto
P1108

Recombinant Human SEPTIN9

Ver Producto
abx032735

Septin 9 (SEPTIN9) Antibody

The maf oncogene was identified by structural analysis of the AS42 avian transforming retrovirus genome. The Maf family is divided into two subclasses, large Mafs (vMaf, cMaf, MafB and Nrl) and small Mafs (MafF, MafK, and MafG). Both subclasses contain leucinezipper motifs, which allow homodimerization as well as heterodimerization with a variety of other bZip transcription factors. Large Mafs also contain an acidic transactivation domain absent in the small Maf proteins. Although they do not possess inherent transactivation activity, small Maf proteins can act as positive regulators of transcription by targeting transcriptionally active dimerization partners to specific DNA regulatory elements. Conversely, small Mafs can act also as negative regulators of transcription by recruiting transcriptional repressors or by forming homodimers that can replace active dimers. Human MafF was isolated in a yeast one-hybrid system from a human myometrium cDNA library. Human MAFF encodes a 164 amino acids proten. Like other small MAFF proteins, it contains an extended leucine zipper structure and lacks an N-terminal transactivating domain. The three small Maf proteins have been implicated in a number of physiological processes, including development, differentiation, haematopoiesis and stress response. Interestingly, these three proteins regulate the stress response via different mechanisms.

Ver Producto