Search: 1000 results found for "Anti Human Heat Shock Protein"

Description:

SUB1 Homolog Human Recombinant

p14, P15, PC4, Positive cofactor 4, SUB1 homolog, RPO2TC1, Activated RNA polymerase II transcriptional coactivator p15, MGC102747.

Product # :

PRO-835

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

SUB1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids (1-127 a.a.) and having a molecular mass of 16.5 kDa. SUB1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

Source

Escherichia Coli.

Formulation

SUB1 Human solution containing 20mM Tris-HCl pH-8, 0.2M NaCl, 5mM DTT & 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
SUB1 is a coactivator that functions together with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. SUB1 interacts with the activation domain of transcription factor IIA (TFIIA) and TATA-binding protein (TBP)-associated factors (TAFs) to directly bind to double stranded DNA. SUB1 induces both activation and repression of RNAPII basal transcription, depending on the presence or absence of these transcription factors and holoenzyme components.
Synonyms
p14, P15, PC4, Positive cofactor 4, SUB1 homolog, RPO2TC1, Activated RNA polymerase II transcriptional coactivator p15, MGC102747.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPKSKELVSS SSSGSDSDSE VDKKLKRKKQ VAPEKPVKKQ KTGETSRALS SSKQSSSSRD DNMFQIGKMR YVSVRDFKGK VLIDIREYWM DPEGEMKPGR KGISLNPEQW SQLKEQISDI DDAVRKL.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Programmed Cell Death 6 Interacting Protein Human Recombinant

AIP1, Alix, PDCD6-Interacting Protein, DRIP4, ALG-2 interacting protein 1, Programmed cell death 6-interacting protein, Hp95, PDCD6IP, KIAA1375, MGC17003.

Product # :

PRO-792

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

PDCD6IP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (1-392 a.a.) and having a molecular mass of 45.8 kDa. The PDCD6IP is fused to a 20 amino acid His-tag at N-terminus and purified by conventional chromatography.

Source

Escherichia Coli.

Formulation

The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
PDCD6IP is a Class E VPS protein which participates in concentration and sorting of cargo proteins of the multivesicular body or incorporation into intralumenal vesicles that are generated by invagination and scission from the limiting membrane of the endosome. PDCD6IP binds to the phospholipid lysobisphosphatidic acid which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. PDCD6IP is an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. PDCD6IP is mandatory for completion of cytokinesis. PDCD6IP takes part in HIV-1 virus budding. PDCD6IP replaces TSG101 in its function of supporting HIV-1 release. PDCD6IP takes part in the regulation of both apoptosis and cell proliferation. PDCD6IP is a cytoplasmic protein that cooperates with apoptosis-associated proteins (ALG-2 and PDCD6) and with the endocytosis-regulator CIN85. Overexpression of PDCD6IP and endophilin
Synonyms
AIP1, Alix, PDCD6-Interacting Protein, DRIP4, ALG-2 interacting protein 1, Programmed cell death 6-interacting protein, Hp95, PDCD6IP, KIAA1375, MGC17003.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MATFISVQLK KTSEVDLAKP LVKFIQQTYP SGGEEQAQYC RAAEELSKLR RAAVGRPLDK HEGALETLLR YYDQICSIEP KFPFSENQIC LTFTWKDAFD KGSLFGGSVK LALASLGYEK SCVLFNCAAL ASQIAAEQNL DNDEGLKIAA KHYQFASGAF LHIKETVLSA LSREPTVDIS PDTVGTLSLI MLAQAQEVFF LKATRDKMKD AIIAKLANQA ADYFGDAFKQ CQYKDTLPKE VFPVLAAKHC IMQANAEYHQ SILAKQQKKF GEEIARLQHA AELIKTVASR YDEYVNVKDF SDKINRALAA AKKDNDFIYH DRVPDLKDLD PIGKATLVKS TPVNVPISQK FTDLFEKMVP VSVQQSLAAY NQRKADLVNR SIAQMREATT LA.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Neurotensin Human Recombinant, sf9

Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.

Product # :

PRO-2374

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

NTS protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

More Info

Introduction
Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in dopamine-associated pathophysiological events, in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.
Synonyms
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH HHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Stathmin Like-2 Human Recombinant

SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 2.

Product # :

PRO-752

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

Recombinant Human Stathmin Like-2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (39-179 a.a) and having a molecular mass of 16.4 kDa. STMN2 is purified by conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

The STMN2 protein solution contains 50mM MES, pH-6.0, 0.1mM PMSF, 1 mM EDTA and 10% Glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
STMN2 is a neuronal growth-associated protein which shares a majority of its amino acid sequence with the phosphoprotein stathmin. STMN2 is involved in neuronal differentiation and in modulating membrane interaction with the cytoskeleton through neurite outgrowth. STMN2 is necessary for maintaining the anchorage-independent growth state of beta-catenin/TCF-activated hepatoma cells. SCG10 is a novel indicator of osteogenesis and osteoblast that takes part in the regulation of the adipocyte/osteoblast balance. STMN2 plays a role as an effector downstream of Rnd1 to regulate axon extensions by modulating microtubule organization.
Synonyms
SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 2.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MDMEVKQINK RASGQAFELI LKPPSPISEA PRTLASPKKK DLSLEEIQKK LEAAEERRKS QEAQVLKQLA EKREHEREVL QKALEENNNF SKMAEEKLIL KMEQIKENRE ANLAAIIERL QEKERHAAEV RRNKELQVEL SG.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

TBP-Like 1 Human Recombinant

TATA box-binding protein-like protein 1, TBP-like protein 1, 21 kDa TBP-like protein, Second TBP of unique DNA protein, STUD, TATA box-binding protein-related factor 2, TBP-related factor 2, TBP-like factor, TBP-related protein, TBPL1, TLF, TLP, TLP21, TRF2, TRP, MGC:8389, MGC:9620.

Product # :

PRO-736

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

TBPL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (1-186 a.a) and having a molecular mass of 23.3kDa.TBPL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TBPL1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 1mM EDTA.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
TBP-Like 1 (TBPL1) is a member of the TBP family. The TATA box-binding protein (TBP) is an indispensable component of the basal transcriptional machinery. TBPL1 is crucial for spermiogenesis and supposed to be significant in expression of developmentally regulated genes.
Synonyms
TATA box-binding protein-like protein 1, TBP-like protein 1, 21 kDa TBP-like protein, Second TBP of unique DNA protein, STUD, TATA box-binding protein-related factor 2, TBP-related factor 2, TBP-like factor, TBP-related protein, TBPL1, TLF, TLP, TLP21, TRF2, TRP, MGC:8389, MGC:9620.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDADSDV ALDILITNVV CVFRTRCHLN LRKIALEGAN VIYKRDVGKV LMKLRKPRIT ATIWSSGKII CTGATSEEEA KFGARRLARS LQKLGFQVIF TDFKVVNVLA VCNMPFEIRL PEFTKNNRPH ASYEPELHPA VCYRIKSLRA TLQIFSTGSI TVTGPNVKAV ATAVEQIYPF VFESRKEIL.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-018

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
biological activity
More Info

Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

More Info

Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Colorless, clear and transparent solution.
Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.

What is the Purity of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.

What applications can G CSF HUMAN, PEG Protein be used in?
G CSF HUMAN, PEG Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Pyruvate Dehydrogenase Complex, Component X, Mouse Anti Human

DLDBP, E3BP, OPDX, PDX1, proX, Component X.

Product # :

ANT-725

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

formulation
More Info

Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

More Info

Introduction
Pyruvate Dehydrogenase Complex, Component X, also known as PDHX, encodes the E3 binding protein subunit of the PDH complex which contains 3 catalytic subunits. PDHX tethers E3 dimers to the E2 core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is critical for a functional PDH complex.
Synonyms
DLDBP, E3BP, OPDX, PDX1, proX, Component X.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human PDHX mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PDHX amino acids 54-501 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
PAT1E11AT
Applications
PDHX antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
PDHX antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Small Ubiquitin-Related Modifier 3 Human Recombinant

SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.

Product # :

PRO-267

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

SUMO3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 112 amino acids (1-92a.a.) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).SUMO3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SUMO3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl,1mM DTT and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
SUMO3 belongs to the SUMO protein family and operates like ubiquitin. Nevertheless, unlike ubiquitin that targets proteins for degradation, SUMO3 protein takes part in several cellular processes, like nuclear transport, transcriptional regulation, apoptosis, and protein stability. SUMO3 regulates amyloid beta generation and is crucial in the onset or progression of Alzheimer’s disease.
Synonyms
SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR FDGQPINETD TPAQLEMEDE DTIDVFQQQT GG

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Heterogeneous Nuclear Ribonucleoprotein A1 Human Recombinant

Heterogeneous nuclear ribonucleoprotein A1, hnRNP A1, Helix-destabilizing protein, Single-strand RNA-binding protein, hnRNP core protein A1, HNRNPA1, HNRPA1, HNRPA1L3, hnRNP-A1.

Product # :

PRO-1038

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

HNRNPA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a.) and having a molecular mass of 36.6kDa.HNRNPA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HNRNPA1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) is a member of the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). HNRNPA1 is involved in the packing of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may control splice site selection. The HNRNPA1 protein may also have a role in HCV RNA replication. In addition, HNRNPA1 is believed to have a key role in the formation of specific myometrial protein species in parturition.
The hnRNP proteins have distinctive nucleic acid binding properties. HNRNPA1 has 2 repeats of quasi-RRM domains that bind to RNAs. HNRNPA1 is one of the most copious core proteins of hnRNP complexes and it is restricted to the nucleoplasm. The HNRNPA1 protein, along with other hnRNP proteins, is exported from the nucleus, most likely bound to mRNA, and is immediately re-imported. The M9 domain of HNRNPA1 functions as both a nuclear localization and nuclear export signal.
Synonyms
Heterogeneous nuclear ribonucleoprotein A1, hnRNP A1, Helix-destabilizing protein, Single-strand RNA-binding protein, hnRNP core protein A1, HNRNPA1, HNRPA1, HNRPA1L3, hnRNP-A1.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSKSESP KEPEQLRKLF IGGLSFETTD ESLRSHFEQW GTLTDCVVMR DPNTKRSRGF GFVTYATVEE VDAAMNARPH KVDGRVVEPK RAVSREDSQR PGAHLTVKKI FVGGIKEDTE EHHLRDYFEQ YGKIEVIEIM TDRGSGKKRG FAFVTFDDHD SVDKIVIQKY HTVNGHNCEV RKALSKQEMA SASSSQRGRS GSGNFGGGRG GGFGGNDNFG RGGNFSGRGG FGGSRGGGGY GGSGDGYNGF GNDGSNFGGG GSYNDFGNYN NQSSNFGPMK GGNFGGRSSG PYGGGGQYFA KPRNQGGYGG SSSSSSYGSG RRF.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

TGFB1-Induced Anti-Apoptotic Factor 1 Human Recombinant

TGFB1-Induced Anti-Apoptotic Factor 1, 12 KDa TGF-Beta-1-Induced Antiapoptotic Factor, Molecule Associated With Jak-3 N-Terminal, KIAA0216, MYO18A, MYSPDZ, MAJN, SPR210.

Product # :

PRO-1211

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

TIAF1 Human Recombinant produced in E. coli is a single polypeptide chain containing 152 amino acids (1-115) and having a molecular mass of 16.6 kDa.TIAF1 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TIAF1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
TGFB1-induced anti-apoptotic factor 1 (TIAF1) hinders the cytotoxic effects of TNF-alpha and overexpressed TNF receptor adapters TRADD, FADD, and RIPK1. The TIAF1 protein is involved in TGF-beta1 inhibition of IkappaB-alpha expression and suppression of TNF-mediated IkappaB-alpha degradation. TIAF1 is not detected in normal kidney and liver. TIAF1 is up-regulated in chronic and acute allograft rejection: expressed in the inflammatory infiltrate and in tubular epithelial cells.
Synonyms
TGFB1-Induced Anti-Apoptotic Factor 1, 12 KDa TGF-Beta-1-Induced Antiapoptotic Factor, Molecule Associated With Jak-3 N-Terminal, KIAA0216, MYO18A, MYSPDZ, MAJN, SPR210.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSS PSSPFREQSF LCAAGDAGEE SRVQVLKNEV RRGSPVLLGW VEQAYADKCV CGPSAPPAPT PPSLSQRVMC NDLFKVNPFQ LQQFRADPST ASLLLCPGGL DHKLNLRGKA WG

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Runt-Related Transcription Factor 3 Human Recombinant

AML2, CBFA3, PEBP2aC, PEBP2A3, FLJ34510, MGC16070, RUNX3, Oncogene AML-2, Runt-related transcription factor 3, Core-binding factor subunit alpha-3, Acute myeloid leukemia 2 protein, Polyomavirus enhancer-binding protein 2 alpha C subunit, SL3-3 enhancer factor 1 alpha C subunit, SL3/AKV core-binding factor alpha C subunit.

Product # :

PRO-836

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

RUNX3 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids (53-186 a.a.) and having a molecular mass of 17.1 kDa. The RUNX3 is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RUNX3 Human solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
RUNX3 is part of the RUNX family that mediates the expression of genes which participate in cellular differentiation and cell cycle progression. RUNX3 heterodimer and the beta subunit form a complex that binds to the core DNA sequence 5''-PYGPYGGT-3'' found in several enhancers and promoters, and can either activate or suppress transcription. RUNX3 interacts with additional transcription factors. RUNX3 is a good candidate for gastric cancer tumor suppressor diagnosis.
Synonyms
AML2, CBFA3, PEBP2aC, PEBP2A3, FLJ34510, MGC16070, RUNX3, Oncogene AML-2, Runt-related transcription factor 3, Core-binding factor subunit alpha-3, Acute myeloid leukemia 2 protein, Polyomavirus enhancer-binding protein 2 alpha C subunit, SL3-3 enhancer factor 1 alpha C subunit, SL3/AKV core-binding factor alpha C subunit.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRSMVDVLAD HAGELVRTDS PNFLCSVLPS HWRCNKTLPV AFKVVALGDV PDGTVVTVMA GNDENYSAEL RNASAVMKNQ VARFNDLRFV GRSGRGKSFT LTITVFTNPT QVATYHRAIK VTVDGPREPR RHRQK.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Myotrophin Human Recombinant

Protein V-1, GCDP, Myotrophin, FLJ31098, FLJ99857.

Product # :

CYT-723

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

MTPN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-118 a.a.) and having a molecular mass of 15 kDa. The MTPN is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MTPN Human solution containing 20mM Tris-HCl pH-8 and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
MTPN is an ankyrin repeat protein, that stimulates protein synthesis and cardiomyocyte growth to commence cardiac hypertrophy by activating the NF-kappaB signaling cascade. Myotrophin participates in cerebellar morphogenesis and takes part in differentiation of cerebellar neurons, particularly of granule cells. High levels of MTPN are expressed in human dilated cardiomyopathic and ischemic hearts.
Synonyms
Protein V-1, GCDP, Myotrophin, FLJ31098, FLJ99857.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTAFEATDN QAIKALLQ.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Bone Morphogenetic protein-3 Human Recombinant

Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

Product # :

CYT-937

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

Purity

Greater than 95.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

More Info

Introduction
Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.
Synonyms
Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.
Background
Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration
Abstract:
Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.
Production of BMP-3 Human Recombinant:
Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.
Potential Therapeutic Applications:
BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.
Conclusion:
BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.
What is the molecular weight/Mw of BMP3 Protein?
BMP3 Protein has a total Mw of 24.8kDa.

What is the source or expression system of BMP3 Protein?
Escherichia Coli.

What is the Purity of BMP3 Protein?
BMP3 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP3 Protein?
The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

What is the amino acid sequence of BMP3 Protein?
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

What applications can BMP3 Protein be used in?
BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP3 Protein?
The endotoxin level is minimal, BMP3 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Guanine Nucleotide Binding Protein Alpha Inhibiting Activity 1 Human Recombinant

Guanine nucleotide-binding protein G(i) subunit alpha-1, Adenylate cyclase-inhibiting G alpha protein, GNAI1, Gi.

Product # :

PRO-940

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

GNAI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 377 amino acids (1-354 a.a.) and having a molecular mass of 42.7kDa.GNAI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GNAI1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Guanine nucleotide binding proteins are heterotrimeric signal-transducing molecules comprising alpha, beta, and gamma subunits. GNAI1 represents the alpha subunit of an inhibitory complex. Guanine nucleotide-binding protein G(i) subunit alpha (GNAI1) functions to transmit information from cell surface receptors to intracellular effectors. GNAI1 binds guanine nucleotide, can hydrolyze GTP, and can interact with other proteins. GNAI1 is part of a complex that responds to beta-adrenergic signals by inhibiting adenylate cyclase. In addition, GNAI1 functions to open atrial potassium channels.
Synonyms
Guanine nucleotide-binding protein G(i) subunit alpha-1, Adenylate cyclase-inhibiting G alpha protein, GNAI1, Gi.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGCTLSA EDKAAVERSK MIDRNLREDG EKAAREVKLL LLGAGESGKS TIVKQMKIIH EAGYSEEECK QYKAVVYSNT IQSIIAIIRA MGRLKIDFGD SARADDARQL FVLAGAAEEG FMTAELAGVI KRLWKDSGVQ ACFNRSREYQ LNDSAAYYLN DLDRIAQPNY IPTQQDVLRT RVKTTGIVET HFTFKDLHFK MFDVGGQRSE RKKWIHCFEG VTAIIFCVAL SDYDLVLAED EEMNRMHESM KLFDSICNNK WFTDTSIILF LNKKDLFEEK IKKSPLTICY PEYAGSNTYE EAAAYIQCQF EDLNKRKDTK EIYTHFTCAT DTKNVQFVFD AVTDVIIKNN LKDCGLF.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Glial Fibrillary Acidic Protein Human Recombinant

Glial fibrillary acidic protein, GFAP

Product # :

PRO-2802

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info

Description

GFAP Human produced in E.coli is a single, non-glycosylated polypeptide chain (60-383 a.a.) and having a molecular mass of 37906 Dalton.

Source

Escherichia Coli.

Formulation

GFAP was lyophilized from 50mM Tris-HCl pH-7.5, 4M Urea 150mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Synonyms
Glial fibrillary acidic protein, GFAP
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GFAP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Glial Fibrillary Acidic Protein should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GFAP in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Glial Fibrillary Acidic Protein (GFAP), a key intermediate filament protein predominantly found in astrocytes, plays a fundamental role in the central nervous system. Initially recognized for its structural functions, GFAP has emerged as a multifaceted molecule with implications in neural development, synaptic plasticity, and various neurological disorders. This research delves into the realm of GFAP human recombinant protein, shedding light on its structural properties, physiological significance, and its diverse roles in both health and disease.
Structural Complexity of GFAP:
GFAP belongs to the family of intermediate filament proteins, conferring structural support to astrocytes. Its unique structure comprises a central α-helical rod domain flanked by non-helical head and tail domains. This structural complexity allows GFAP to form stable filaments, providing structural integrity to astrocytes and contributing to the architecture of the central nervous system.
Physiological Functions in Glial Cells:
Beyond its structural role, GFAP participates in various physiological processes within glial cells. It is involved in the regulation of astrocyte morphology, motility, and migration, crucial for their interactions with neurons and blood vessels. Additionally, GFAP contributes to the formation and maintenance of the blood-brain barrier, highlighting its significance in the brain's homeostasis.
Implications in Neurological Disorders:
Aberrant GFAP expression and aggregation are associated with several neurological disorders. In Alexander disease, a rare neurodegenerative disorder, mutations in the GFAP gene lead to the formation of GFAP aggregates, contributing to disease pathology. Moreover, elevated levels of GFAP in cerebrospinal fluid serve as a biomarker for various neurological conditions, including traumatic brain injury, Alzheimer's disease, and multiple sclerosis, indicating its involvement in the brain's response to injury and neuroinflammation.
GFAP in Neural Regeneration:
Recent studies have unveiled GFAP’s role in neural regeneration and repair processes. In response to brain injury, GFAP-expressing astrocytes become reactive, forming a glial scar that isolates damaged areas. While this scar formation initially limits tissue damage, persistent scar formation can impede neural regeneration. Understanding the dynamics of GFAP expression in reactive astrocytes is crucial for developing therapies that promote neural regeneration following brain injuries or neurodegenerative diseases.
GFAP human recombinant protein, once thought of as a structural element in astrocytes, has proven to be a pivotal player in the complex landscape of glial biology and neurological disorders. Its intricate functions extend beyond providing structural support, encompassing roles in neural development, disease pathology, and tissue repair. As research continues to uncover the nuances of GFAP’s involvement in health and disease, it offers promising avenues for developing targeted therapies and diagnostic tools, emphasizing its significance in the intricate workings of the central nervous system.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Indian Hedgehog Human Recombinant

Indian hedgehog protein, IHH, HHG-2, BDA1.

Product # :

CYT-195

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

IHH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8kDa. The IHH is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED₅₀ for this effect is 3.0-10.0?g/ml corresponding to a specific activity of 100-334units/mg.

More Info

Introduction
IHH belongs to the hedgehog family of secreted signaling molecules. Hedgehog proteins are vital regulators of various developmental processes including growth, patterning and morphogenesis. The vertebrate homologues of Hh comprise several proteins including sonic hedgehog (Shh), Indian hedgehog (Ihh), and Desert hedgehog (Dhh). IHH has a specific role in bone growth and differentiation. In addition, IHH is involved in yolk sac vasculogenesis, having a central role in differentiation of epiblast cells into endothelial and red blood cells. IHH mRNA expression is detected in fetal lung, gut, stomach, liver, kidney, pancreas and strongly in cartilage in growth regions of the developing bone. IHH gene mutations cause the brachydactyly type A1 which is characterized by shortening or malformation of the phalanges and also the acrocapitofemoral dysplasia.
Synonyms
Indian hedgehog protein, IHH, HHG-2, BDA1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IHH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IHH should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IHH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IIGPGRVVGS RRRPPRKLVP LAYKQFSPNV PEKTLGASGR YEGKIARSSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDRLNSLAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRNKYGLL ARLAVEAGFD WVYYESKAHV HCSVKSEHSA AAKTGG.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Histidine Triad Nucleotide Binding Protein 1 Human Recombinant

HINT, PKCI-1, PRKCNH1, FLJ30414, FLJ32340, HINT1, Histidine triad nucleotide-binding protein 1, Adenosine 5'-monophosphoramidase, Protein kinase C inhibitor 1, Protein kinase C-interacting protein 1, PKCI1.

Product # :

PRO-702

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

HINT1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 126 amino acids (1-126 a.a.) and having a molecular mass of 13.8 kDa.The HINT1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HINT1 solution contains 20mM Tris pH-8 & 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
HINT1, also known as Histidine triad nucleotide-binding protein 1 is part of the superfamily named for a near C-terminal HXHXHXX motif (H:Histidine, X:a hydrophobic amino acid) positioned at the ?-phosphate of nucleotide substrates. HINT1 hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2. Though it was initially considered to be a protein kinase C inhibitor and act as a haplod-insufficient tumor suppressor including spontaneous tumor formation in Hint+/- and Hint-/- , its actual physiologic function is not known.
Synonyms
HINT, PKCI-1, PRKCNH1, FLJ30414, FLJ32340, HINT1, Histidine triad nucleotide-binding protein 1, Adenosine 5'-monophosphoramidase, Protein kinase C inhibitor 1, Protein kinase C-interacting protein 1, PKCI1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MADEIAKAQV ARPGGDTIFG KIIRKEIPAK IIFEDDRCLA FHDISPQAPT HFLVIPKKHI SQISVAEDDD ESLLGHLMIV GKKCAADLGL NKGYRMVVNE GSDGGQSVYH VHLHVLGGRQ MHWPPG.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Tyr-3/Trp-5 Monooxygenase Activation Protein, Epsilon Human Recombinant, His Tag

YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon, HEL2, KCIP-1, MDCR, MDS.

Product # :

PKA-095

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

YWHAE Human Recombinant produced in E. coli is a single polypeptide chain containing 275 amino acids (1-255) and having a molecular mass of 31.3kDa. YWHAE is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The YWHAE solution (1mg/1ml) contains phosphate buffered Saline (pH7.4), 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ and η that have been identified in mammals. The 14-3-3 epsilon, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of insulin sensitivity. It has also been implicated in the pathogenesis of small cell lung cancer.
Synonyms
YWHAE, MDS, MDCR, KCIP-1, 14-3-3E, 14-3-3 Epsilon, FLJ45465, Tyr-3/Trp- 5 Monooxygenase Activation Protein Epsilon, HEL2, KCIP-1, MDCR, MDS.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Purine-Rich Element Binding Protein B Human Recombinant

Transcriptional activator protein Pur-beta, Purine-rich element-binding protein B, PURB, PURBETA.

Product # :

PRO-1969

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

PURB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312) and having a molecular mass of 35.6 kDa.PURB is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The PURB solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Purine-Rich Element Binding Protein B (PURB) is a single-stranded DNA-binding protein which takes part in the dendritic transport of a subset of mRNAs. PURB operates as repressor in myoblasts and fibroblasts in the control of vascular smooth muscle alpha-actin gene transcription. PURB binds preferentially to the single strand of the purine-rich element termed PUR, which is present at origins of replication and in gene flanking regions in various eukaryotes from yeasts through humans.
Synonyms
Transcriptional activator protein Pur-beta, Purine-rich element-binding protein B, PURB, PURBETA.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMADGDSG SERGGGGGPC GFQPASRGGG EQETQELASK RLDIQNKRFY LDVKQNAKGR FLKIAEVGAG GSKSRLTLSM AVAAEFRDSL GDFIEHYAQL GPSSPEQLAA GAEEGGGPRR ALKSEFLVRE NRKYYLDLKE NQRGRFLRIR QTVNRGGGGF GAGPGPGGLQ SGQTIALPAQ GLIEFRDALA KLIDDYGGED DELAGGPGGG AGGPGGGLYG ELPEGTSITV DSKRFFFDVG CNKYGVFLRV SEVKPSYRNA ITVPFKAWGK FGGAFCRYAD EMKEIQERQR DKLYERRGGG SGGGEESEGE EVDED.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Activin-A Human Recombinant, Plant-Active

Inhba, Inhibin beta A, FSH releasing protein.

Product # :

CYT-414

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.

Source

Nicotiana benthamiana.

Formulation

Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4

Purity

Greater than 98% as obsereved by SDS-PAGE.

Biological Activity

The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([³H]thymidine incorporation). ED₅₀<5ng/ml.

More Info

Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
Physical Appearance
Lyophilized freeze dried powder.
Stability
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.
Solubility
INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.
Amino Acid Sequence
HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 27.4 kDa.
What is the source or expression system of Activin A Protein?
Nicotiana benthamiana.
What is the Purity of Activin A Protein?
Activin A Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of Activin A Protein?
The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.
What is the endotoxin level for Activin A Protein?
The endotoxin level is minimal, ACTIVIN A Protein was purified using conventional chromatography techniques.
What is the amino acid sequence of ACTIVIN A Protein?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
What applications can ACTIVIN-A Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Small Nuclear Ribonucleoprotein Polypeptide D3 Human Recombinant, Sf9

Small nuclear ribonucleoprotein D3 polypeptide 18kDa, Sm-D3, snRNP core protein D3.

Product # :

PRO-996

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

SNRPD3 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 18 KDa. SNRPD3 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Sf9 insect cells.

Formulation

SNRPD3 is supplied in 20mM HEPES buffer pH-7.5, 400mM NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
SNRPD3 is a small nuclear ribonucleoprotein (snRNPs) that contains the spliceosome in eukaryotes. SNRPD3 is essential for pre-mRNA splicing and small nuclear ribonucleoprotein biogenesis. Alternative splicing happens in this locus and two transcript variants encoding the same protein were branded.
Synonyms
Small nuclear ribonucleoprotein D3 polypeptide 18kDa, Sm-D3, snRNP core protein D3.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative samples).
coating concentration
0.4-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.
Applications
Western blot with anti-Sm positive patient sera.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibroblast Growth Factor Basic 147 a.a. Human Recombinant

Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.

Product # :

CYT-557

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16.5kDa. The FGF2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The bFGF was lyophilized from a sterile filtered solution containing 20mM Tris-HCl, pH 7.6 and 150mM NaCl.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x10⁷ units/mg.

More Info

Introduction
FGF-basic is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized basic-FGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGFb should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized FGF-B in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.
Background
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 16.5kDa.

What is the source or expression system of FGF 2 Protein?
Escherichia Coli.

What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 2 Protein?
The ED50, Calculated by the dose- dependent proliferation of mouse BALB/c 3T3 cells is < 0.05ng/ml corresponding to a specific activity of 2.0x107 units/mg.

What is the amino acid sequence of FGF 2 Protein?
MPALPEDGGS GAFPPGHFKD PKRLYCKNGG FFLRIHPDGR VDGVREKSDP HIKLQLQAEE RGVVSIKGVC ANRYLAMKED GRLLASKCVT DECFFFERLE SNNYNTYRSR KYTSWYVALK RTGQYKLGSK TGPGQKAILF LPMSAKS.

What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

B-cell Activating Factor Receptor Human Recombinant

TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.

Product # :

CYT-429

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

B Lymphocyte Stimulator Receptor Human Recombinant extracellular produced in E.Coli is a single, non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of 7.7 kDa.The BAFF-R is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 8.0, 500mM NaCl.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to block BAFF induced mouse splenocyte survival. The expected ED₅₀ for this effect is 1.0-5.0 µg/ml in the presence of 1.0µg/ml of human soluble BAFF.

More Info

Introduction
B cell-activating factor (BAFF) enhances B-cell survival in vitro and is a regulator of the peripheral B-cell population. Overexpression of Baff in mice results in mature B-cell hyperplasia and symptoms of systemic lupus erythematosus (SLE). Also, some SLE patients have increased levels of BAFF in serum. Therefore, it has been proposed that abnormally high levels of BAFF may contribute to the pathogenesis of autoimmune diseases by enhancing the survival of autoreactive B cells. The protein encoded by this gene is a receptor for BAFF and is a type III transmembrane protein containing a single extracellular cysteine-rich domain. It is thought that this receptor is the principal receptor required for BAFF-mediated mature B-cell survival.
Synonyms
TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BAFF-R although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution B Lymphocyte Stimulator Receptor should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized B Lymphocyte Stimulator Receptor Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRRGPRSLRGRDAPAPTPCVPAECFDLLVRHCVACGLLRTPRPKPAG
ASSPAPRTALQPQESVGAGAGEAALPLPG.
Background
B-cell Activating Factor Receptor Human Recombinant: Unlocking the Potential of a Key Immunomodulatory Target
Abstract:
B-cell Activating Factor Receptor (BAFF-R) human recombinant is a critical component of the B-cell immune response, playing a pivotal role in B-cell survival, maturation, and antibody production. This research paper provides a comprehensive analysis of BAFF-R, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BAFF-R human recombinant are proposed, shedding light on its future implications in the field of immunotherapy.
Introduction:
The immune system relies on the precise regulation of B-cell functions, with BAFF-R serving as a key modulator of B-cell development and activation. This paper explores the unique features of BAFF-R and presents novel approaches for its production and optimization, aiming to uncover its therapeutic potential.
Characteristics and Signaling Pathways:
BAFF-R is a type III transmembrane protein expressed primarily on B-cells. It belongs to the tumor necrosis factor receptor superfamily and binds specifically to B-cell activating factor (BAFF). Engagement of BAFF-R by BAFF initiates intracellular signaling cascades, including the activation of nuclear factor-kappa B (NF-κB) and mitogen-activated protein kinase (MAPK) pathways, promoting B-cell survival, proliferation, and differentiation.
Production of BAFF-R Human Recombinant:
Efficient production methodologies are crucial for the therapeutic application of BAFF-R human recombinant. Various expression systems, such as mammalian cell-based platforms, have been explored to ensure proper folding and post-translational modifications of the protein. Optimization strategies, including codon optimization and vector design, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to isolate high-quality BAFF-R recombinant.
Potential Therapeutic Applications:
BAFF-R human recombinant holds great promise in the field of immunotherapy. Dysregulation of the BAFF/BAFF-R signaling axis has been implicated in autoimmune diseases, such as systemic lupus erythematosus and rheumatoid arthritis. Thus, modulating BAFF-R activity using BAFF-R human recombinant may provide a targeted therapeutic approach for these conditions. Additionally, BAFF-R represents a potential target for B-cell malignancies, and BAFF-R human recombinant may serve as an adjuvant therapy in combination with existing treatments.
Conclusion:
BAFF-R human recombinant represents a crucial immunomodulatory target with diverse therapeutic applications in immunotherapy. Optimizing production methodologies and further understanding its signaling pathways will enhance its clinical utility. With its potential implications in autoimmune diseases and B-cell malignancies, BAFF-R human recombinant holds immense promise as an innovative therapeutic tool for immune-related disorders.
What is the molecular weight/Mw of BAFF R Protein?
BAFF R Protein has a total Mw of 7.7kDa.

What is the source or expression system of BAFF R Protein?
Escherichia Coli.

What is the Purity of BAFF R Protein?
BAFF R Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BAFF R Protein?
Determined by its ability to block BAFF induced mouse splenocyte survival. The expected ED50 for this effect is 1.0-5.0 µg/ml in the presence of 1.0µg/ml of human soluble BAFF.

What is the amino acid sequence of BAFF R Protein?
MRRGPRSLRGRDAPAPTPCVPAECFDLLVRHCVACGLLRTPRPKPAG
ASSPAPRTALQPQESVGAGAGEAALPLPG.

What applications can BAFF R Protein be used in?
BAFF R Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BAFF R Protein?
The endotoxin level is minimal, BAFF R Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Syntaxin-4 Human Recombinant

Syntaxin 4, syntaxin 4A (placental), STX4A, Renal carcinoma antigen NY-REN-31, p35-2.

Product # :

PRO-1176

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

STX4 Human Recombinant produced in E. coli is a single polypeptide chain containing 300 amino acids (1-275) and having a molecular mass of 34.7 kDa.STX4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The STX4 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 40% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Syntaxin 4 (STX4) is a member of the syntaxin/epimorphin family of proteins. The Syntaxin family is cellular receptors for transport vesicles which participate in exocytosis in neutrophils. Syntaxin 4 is vital for normal regulation of glucose metabolism uptake in skeletal muscle and decline in STX4 protein levels lead to reduction of whole-body hormone-stimulated glucose metabolism. STX4 is expressed in neutrophils and neutrophil-differentiated HL-60 cells. The STX4 expression in neutrophils increases with differentiation.
Synonyms
Syntaxin 4, syntaxin 4A (placental), STX4A, Renal carcinoma antigen NY-REN-31, p35-2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMMRDRT HELRQGDDSS DEEDKERVAL VVHPGTARLG SPDEEFFHKV RTIRQTIVKL GNKVQELEKQ QVTILATPLP EESMKQELQN LRDEIKQLGR EIRLQLKAIE PQKEEADENY NSVNTRMRKT QHGVLSQQFV ELINKCNSMQ SEYREKNVER IRRQLKITNA GMVSDEELEQ MLDSGQSEVF VSNILKDTQV TRQALNEISA RHSEIQQLER SIRELHDIFT FLATEVEMQG EMINRIEKNI LSSADYVERG QEHVKTALEN QKKARKKKVL

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Country/region

Search results

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Formulation

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info