Search: 773 results found for "Basic Transcription Factor"

Description:

Stromal Cell-Derived Factor 2 Human Recombinant

Stromal cell-derived factor 2, SDF-2.

Product # :

CHM-028

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Description

SDF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (19-211 a.a) and having a molecular mass of 23.7kDa. SDF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SDF2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Stromal Cell-Derived Factor 2 (SDF2) is a secretory protein which is partly similar to the hydrophilic segments of yeast mannosyltransferases. SDF2 protein’s expression is ubiquitous and the gene is rather conserved among mammals. SDF2is a protein-coding gene whose alternative splicing results in coding and non-coding variants.
Synonyms
Stromal cell-derived factor 2, SDF-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 MGSSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAEL.
Background
What is the molecular weight/Mw of SDF2 HUMAN Protein?
SDF2 HUMAN Protein has a total Mw of 23.7kDa.

What is the source or expression system of SDF2 HUMAN Protein?
Escherichia Coli.

What is the Purity of SDF2 HUMAN Protein?
SDF2 HUMAN Protein is > 85% pure as determined by SDS-PAGE.

What is the Biological Activity of SDF2 HUMAN Protein?
The biological functionality of SDF2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of SDF2 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAEL.

What applications can SDF2 HUMAN Protein be used in?
SDF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for SDF2 HUMAN Protein?
The endotoxin level is minimal, SDF2 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant SDF2 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of SDF2 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Stromal Cell-Derived Factor-1 alpha Human Recombinant, His Tag

SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.

Product # :

CHM-241

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Description

Stromal Cell-Derived Factor-1 alpha Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 78 amino acids, having a molecular mass of 9.2 kDa. The SDF-1a is fused to 10 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was filtered (0.4µm) and lyophilized from a concentrated (0.5mg/ml) solution containing 20mM Tris buffer pH-7.5 and 20mM sodium chloride.

Purity

Greater than 95.0% as determined SDS-PAGE.

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Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK.
Background
What is the molecular weight/Mw of CXCL12 HUMAN ALPHA, HIS Protein?
CXCL12 HUMAN ALPHA, HIS Protein has a total Mw of 9.2kDa.

What is the source or expression system of CXCL12 HUMAN ALPHA, HIS Protein?
Escherichia Coli.

What is the Purity of CXCL12 HUMAN ALPHA, HIS Protein?
CXCL12 HUMAN ALPHA, HIS Protein is > 95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 HUMAN ALPHA, HIS Protein?
The biological functionality of CXCL12 HUMAN ALPHA, HIS Protein will be determined in the future.

What is the amino acid sequence of CXCL12 HUMAN ALPHA, HIS Protein?
MKHHHHHHAS KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE YLEKALNK.

What applications can CXCL12 HUMAN ALPHA, HIS Protein be used in?
CXCL12 HUMAN ALPHA, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL12 HUMAN ALPHA, HIS Protein?
The endotoxin level is minimal, CXCL12 HUMAN ALPHA, HIS Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL12 HUMAN ALPHA, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL12 HUMAN ALPHA, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Pentraxin-3 Human Recombinant

TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.

Product # :

PRO-694

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Description

Recombinant Human PTX3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (18-381 a.a) and having a molecular mass of 44.4 kDa. PTX3 is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PTX3 protein contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by Analysis by SDS-PAGE.

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Introduction
PTX3 is part of the pentraxin family sharing the C-terminal domain with short pentraxins and containing a unique N-terminal domain. PTX3 is produced and released at inflammatory sites by various cell types including monocytes/macrophages, endothelial cells, vascular smooth muscle cells, fibroblasts, and adipocytes. PTX3 is involved in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. PTX3 is used as a marker for disease activity of psoriasis. High serum PTX3 levels are associated with the disease severity of systemic sclerosis. Elevated serum PTX3 is associated with pulmonary fungal infections.
Synonyms
TSG-14, TNFAIP5, PTX3, Pentraxin-related protein PTX3, Pentaxin-related protein PTX3, Tumor necrosis factor-inducible gene 14 protein, TSG14, pentraxin-related gene rapidly induced by IL-1 beta.
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 KDRWGSMENS DDYDLMYVNL DNEIDNGLHP TEDPTPCDCG QEHSEWDKLF IMLENSQMRE RMLLQATDDV LRGELQRLRE ELGRLAESLA RPCAPGAPAE ARLTSALDEL LQATRDAGRR LARMEGAEAQ RPEEAGRALA AVLEELRQTR ADLHAVQGWA ARSWLPAGCE TAILFPMRSK KIFGSVHPVR PMRLESFSAC IWVKATDVLN KTILFSYGTK RNPYEIQLYL SYQSIVFVVG GEENKLVAEA MVSLGRWTHL CGTWNSEEGL TSLWVNGELA ATTVEMATGH IVPEGGILQI GQEKNGCCVG GGFDETLAFS GRLTGFNIWD SVLSNEEIRE TGGAESCHIR GNIVGWGVTE IQPHGGAQYV S.

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:

Leptin Chicken Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-505

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Description

Leptin Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

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

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity is however 5-10 fold lower as compared to mammalian leptins.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Cys-Gln.
Recombinant Chicken leptin was produced according to the a.a. sequence published by the groups of Taouis & McMutry, see Raver et al. Protein Expr Purif. 1998 Dec; 14(3):403-8.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.19 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Chicken as a Reference Standard.

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:

Platelet-derived Growth Factor AA Human Recombinant, Yeast

Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.

Product # :

CYT-568

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Description

PDGF-AA Human Recombinant produced in Yeast is a homodimeric, glycosilated, polypeptide chain containing 2 x 110 amino acids and having a total molecular mass of 34 kDa. PDGF-AA is purified by proprietary chromatographic techniques.

Source

Pichia Pastoris.

Formulation

The protein was lyophilized with 20mM sodium phosphate buffer.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

The ED50 was found to be 1ng/ml corresponding to a Specific Activity of 1,000,000IU/mg calculated by the ability to stimulate the proliferation of mouse 3T3 fibroblasts (PNAS 94, 10205, 1997. Biochemistry, 1996, 35, 12077).

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Introduction
PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, PDGF-AA, PDGF-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PDGF-AA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-AA 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 PDGF-AA in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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:

GDNF Family Receptor Alpha 3 Human Recombinant, Sf9

GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor, GFRA3.

Product # :

CYT-1013

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Description

GFRA3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 585 amino acids (32-374) and having a molecular mass of 65.5kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA3 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GFRA3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
GDNF Family Receptor Alpha 3 (GFRA3) belongs to the GDNF receptor family. GFRA3 creates a signaling receptor complex with RET tyrosine kinase receptor and binds the ligand, artemin (ARTN).
Synonyms
GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor, GFRA3.
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
ADPDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSG PHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVM AHQNENLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
Background
What is the molecular weight/Mw of GFRA3 HUMAN, SF9 Protein?
GFRA3 HUMAN, SF9 Protein has a total Mw of 65.5kDa.

What is the source or expression system of GFRA3 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.
What is the Purity of GFRA3 HUMAN, SF9 Protein?
GFRA3 HUMAN, SF9 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of GFRA3 HUMAN, SF9 Protein?
The biological functionality of GFRA3 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of GFRA3 HUMAN, SF9 Protein?
ADPDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSG PHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVM AHQNENLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

What applications can GFRA3 HUMAN, SF9 Protein be used in?
GFRA3 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GFRA3 HUMAN, SF9 Protein?
The endotoxin level is minimal, GFRA3 HUMAN, SF9 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:

Granulocyte Colony Stimulating Factor, Mouse Anti-Human, Biotin

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

Product # :

ANT-240

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Formulation

1 mg/ml in PBS (after reconstitution).

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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.
Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human G-CSF.
Ig Subclass
Mouse IgG.
Clone
NYRhGCSF.
Applications
Direct ELISA, Western Blot, Intra-cellular staining.
Titer
For intra-cellular staining use 10µl per 1,000,000 cells.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Protein A.

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:

U2 Small Nuclear RNA Auxiliary Factor 1 Human Recombinant

Splicing factor U2AF 35 kDa subunit, U2 auxiliary factor 35 kDa subunit, U2 small nuclear RNA auxiliary factor 1, U2 snRNP auxiliary factor small subunit, U2AF35, U2AFBP, FP793, RNU2AF1, RN.

Product # :

PRO-1461

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Description

U2AF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (1-240 a.a) and having a molecular mass of 30.3kDa.U2AF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

U2AF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
U2AF1 is a member of the splicing factor SR family. U2 auxiliary factor, comprising a large and asmall subunit, is a non-snRNP protein essential for the binding of U2 snRNP to the pre-mRNA branch site.U2AF1 is the small subunit which plays a vital role in both constitutive and enhancer-dependent RNA splicing bydirectly mediating interactions between the large subunit and proteins bound to the enhancers. U2 small nuclear RNA auxiliary factor 1 (U2AF1) is a protein-coding gene. Among the diseases which are associated with U2AF1:Myoclonus Epilepsy and progressive Myoclonus Epilepsy.
Synonyms
Splicing factor U2AF 35 kDa subunit, U2 auxiliary factor 35 kDa subunit, U2 small nuclear RNA auxiliary factor 1, U2 snRNP auxiliary factor small subunit, U2AF35, U2AFBP, FP793, RNU2AF1, RN.
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 MGSMAEYLAS IFGTEKDKVN CSFYFKIGAC RHGDRCSRLH NKPTFSQTIL IQNIYRNPQN SAQTADGSHC AVSDVEMQEH YDEFFEEVFT EMEEKYGEVE EMNVCDNLGD HLVGNVYVKF RREEDAEKAV IDLNNRWFNG QPIHAELSPV TDFREACCRQ YEMGECTRGG FCNFMHLKPI SRELRRELYG RRRKKHRSRS RSRERRSRSR DRGRGGGGGG GGGGGGRERD RRRSRDRERS GRF

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:

Vascular Endothelial Growth Factor Receptor-1 Human Recombinant

FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.

Product # :

PKA-240

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Description

Soluble FLT1 Human Recombinant produced in baculovirus is monomeric, glycosylated, polypeptide containing 687 amino acids and having a molecular mass of 96 kDa. The soluble receptor protein contains only the first 6 extracellular domains, which contain all the information necessary for binding of VEGF.The FLT1 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

FLT1 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

Purity

Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The activity of FLT1 was determined by its ability to inhibit the VEGF (165)-induced proliferation of HUVECs.

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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor.
Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT1 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 FLT1 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRGEHC NKKAVFSRIS KFKSTRNDCT TQSNVKH

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:

Insulin-Like Growth Factor 1 Mouse Recombinant

Somatomedin C, IGF-I, IGFIA, IGF1.

Product # :

CYT-229

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Description

Insulin-Like Growth Factor I mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7600 Dalton. IGF-I is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 1.0 ng/ml, corresponding to a specific activity of 1MU/mg.

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Introduction
The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).
Synonyms
Somatomedin C, IGF-I, IGFIA, IGF1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGFI although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF-1 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 IGF1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Glu-Thr-Leu.
Background
What is the molecular weight/Mw of IGF1 MOUSE Protein?
IGF1 MOUSE Protein has a total Mw of 7.6kDa.

What is the source or expression system of IGF1 MOUSE Protein?
Escherichia Coli.

What is the Purity of IGF1 MOUSE Protein?
IGF1 MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IGF1 MOUSE Protein?
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 1.0 ng/ml, corresponding to a specific activity of 1MU/mg.

What is the amino acid sequence of IGF1 MOUSE Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Glu-Thr-Leu.

What applications can IGF1 MOUSE Protein be used in?
IGF1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGF1 MOUSE Protein?
The endotoxin level is minimal, IGF1 MOUSE Protein was purified using conventional chromatography techniques.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.47 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IGF-I as a Reference Standard.

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:

Retinoblastoma Binding Protein 4 Human Recombinant

Histone-binding protein RBBP4, Chromatin assembly factor 1 subunit C, CAF-1 subunit C, Chromatin assembly factor I p48 subunit, CAF-I 48 kDa subunit, CAF-I p48, Nucleosome-remodeling factor subunit RBAP48, Retinoblastoma-binding protein 4, RBBP-4, Retinoblastoma-binding protein p48, RBBP4, RBAP48, NURF55.

Product # :

PRO-1168

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Description

RBBP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 449 amino acids (1-425 a.a) and having a molecular mass of 50.2kDa.RBBP4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

RBBP4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM EDTA.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Retinoblastoma binding protein 4 (RBBP4) is a ubiquitously expressed nuclear protein which is a member of a highly conserved subfamily of WD-repeat proteins. RBBP4 is present in protein complexes involved in histone acetylation and chromatin assembly. In addition, RBBP4 is part of co-repressor complexes, which is a fundamental component of transcriptional silencing. RBBP4 is observed among several cellular proteins which bind directly to a retinoblastoma protein to regulate cell proliferation. RBBP4 also is a part of the Mi-2 complex which is implicated in chromatin remodeling and transcriptional repression connected with histone deacetylation.
Synonyms
Histone-binding protein RBBP4, Chromatin assembly factor 1 subunit C, CAF-1 subunit C, Chromatin assembly factor I p48 subunit, CAF-I 48 kDa subunit, CAF-I p48, Nucleosome-remodeling factor subunit RBAP48, Retinoblastoma-binding protein 4, RBBP-4, Retinoblastoma-binding protein p48, RBBP4, RBAP48, NURF55.
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 MGSHMADKEA AFDDAVEERV INEEYKIWKK NTPFLYDLVM THALEWPSLT AQWLPDVTRP EGKDFSIHRL VLGTHTSDEQ NHLVIASVQL PNDDAQFDAS HYDSEKGEFG GFGSVSGKIE IEIKINHEGE VNRARYMPQN PCIIATKTPS SDVLVFDYTK HPSKPDPSGE CNPDLRLRGH QKEGYGLSWN PNLSGHLLSA SDDHTICLWD ISAVPKEGKV VDAKTIFTGH TAVVEDVSWH LLHESLFGSV ADDQKLMIWD TRSNNTSKPS HSVDAHTAEV NCLSFNPYSE FILATGSADK TVALWDLRNL KLKLHSFESH KDEIFQVQWS PHNETILASS GTDRRLNVWD LSKIGEEQSP EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWVICSVSED NIMQVWQMAE NIYNDEDPEG SVDPEGQGS.

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 Receptor-4 Human Recombinant, His Tag

Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.

Product # :

PKA-090

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Description

Fibroblast Growth Factor Receptor-4 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (22-369a.a.) and having a molecular mass of 39.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).FGFR4 is fused with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FGFR4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Fibroblast growth factors (FGFs) comprise a family of at least eighteen structurally related proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentiation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family of type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGF R1 - 4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid-box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain. Multiple forms of FGF R1 - 3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGF R1 and 2 results in receptors containing all three Ig domains, referred to as the a isoform, or only IgII and IgIII, referred to as the b isoform. Only the a isoform has been identified for FGF R3 and FGF R4. Additional splicing events for FGF R1 - 3, involving the C-terminal half of the IgIII domain encoded by two mutually exclusive alternative exons, generate FGF receptors with alternative IgIII domains (IIIb and IIIc). A IIIa isoform which is a secreted FGF binding protein containing only the N-terminal half of the IgIII domain plus some intron sequences has also been reported for FGF R1. Mutations in FGF R1 - 3 have been found in patients with birth defects involving craniosynostosis. The complex patterns of expression of these receptors as well as the specificity of their interactions with the various FGF ligand family members are under investigation.
Synonyms
Fibroblast Growth Factor Receptor 4, EC 2.7.10.1, JTK2, TKF, Tyrosine Kinase Related To Fibroblast Growth Factor Receptor, Hydroxyaryl-Protein Kinase, Protein-Tyrosine Kinase, Tyrosylprotein Kinase, CD334 Antigen, EC 2.7.10, FGFR-4, CD334, FGFR4.
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
LEASEEVELE PCLAPSLEQQ EQELTVALGQ PVRLCCGRAE RGGHWYKEGS RLAPAGRVRG WRGRLEIASF LPEDAGRYLC LARGSMIVLQ NLTLITGDSL TSSNDDEDPK SHRDPSNRHS YPQQAPYWTH PQRMEKKLHA VPAGNTVKFR CPAAGNPTPT IRWLKDGQAF HGENRIGGIR LRHQHWSLVM ESVVPSDRGT YTCLVENAVG SIRYNYLLDV LERSPHRPIL QAGLPANTTA VVGSDVELLC KVYSDAQPHI QWLKHIVING SSFGADGFPY VQVLKTADIN SSEVEVLYLR NVSAEDAGEY TCLAGNSIGL SYQSAWLTVL PEEDPTWTAA APEARYTDLE HHHHHH.

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:

DIM1 Dimethyladenosine Transferase 1 Human Recombinant

Probable dimethyladenosine transferase, DIM1 dimethyladenosine transferase 1 homolog, DIM1 dimethyladenosine transferase 1-like, Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase, Probable 18S rRNA dimethylase, Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase, DIMT1, DIMT1L, HUSSY-05, HSA9761.

Product # :

ENZ-628

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Description

DIMT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-313) and having a molecular mass of 37.5kDa.DIMT1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The DIMT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 30% glycerol, 2mM DTT, 200mM NaCl and 2mM EDTA.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
DIM1 dimethyladenosine transferase 1 homolog (DIMT1) is a member of the methyltransferase superfamily. The DIMT1 enzyme specifically dimethylates 2 adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. DIMT1 is restricted to the nucleolus.
Synonyms
Probable dimethyladenosine transferase, DIM1 dimethyladenosine transferase 1 homolog, DIM1 dimethyladenosine transferase 1-like, Probable 18S rRNA (adenine(1779)-N(6)/adenine(1780)-N(6))-dimethyltransferase, Probable 18S rRNA dimethylase, Probable S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase, DIMT1, DIMT1L, HUSSY-05, HSA9761.
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 MMPKVKSGAI GRRRGRQEQR RELKSAGGLM FNTGIGQHIL KNPLIINSII DKAALRPTDV VLEVGPGTGN MTVKLLEKAK KVVACELDPR LVAELHKRVQ GTPVASKLQV LVGDVLKTDL PFFDTCVANL PYQISSPFVF KLLLHRPFFR CAILMFQREF ALRLVAKPGD KLYCRLSINT QLLARVDHLM KVGKNNFRPP PKVESSVVRI EPKNPPPPIN FQEWDGLVRI TFVRKNKTLS AAFKSSAVQQ LLEKNYRIHC SVHNIIIPED FSIADKIQQI LTSTGFSDKR ARSMDIDDFI RLLHGFNAEG IHFS.

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 EDRK-Rich Factor 2 Human Recombinant

Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.

Product # :

PRO-1730

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Description

SERF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 82 amino acids (1-59 a.a) and having a molecular mass of 9.3kDa.SERF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SERF2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
SERF2 (small EDRK-rich factor 2) is a member of the SERF family. SERF2 is a protein-coding gene. Among the diseases associated with SERF2 are spinal muscular atrophy, and muscular atrophy.
Synonyms
Small EDRK-rich factor 2, Gastric cancer-related protein VRG107, Protein 4F5-related, 4F5re, h4F5rel, FAM2C, HsT17089.
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 MGSMTRGNQR ELARQKNMKK QSDSVKGKRR DDGLSAAARK QRDSEIMQQK QKKANEKKEE PK

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:

Growth and Differentiation factor 11 Human Recombinant, His Tag

Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.

Product # :

CYT-887

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Description

GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (299-407a.a) and having a molecular mass of 14.8kDa. GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF11 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
Synonyms
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
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 MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
Background
What is the molecular weight/Mw of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein has a total Mw of 14.8kDa.

What is the source or expression system of GDF11 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF11 HUMAN, HIS Protein?
The biological functionality of GDF11 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of GDF11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.

What applications can GDF11 HUMAN, HIS Protein be used in?
GDF11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF11 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF11 HUMAN, HIS 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:

Growth differentiation factor 5 Human Recombinant, His Tag

Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.

Product # :

CYT-653

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Description

GDF5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (382-501 a.a.) and having a total molecular mass of 15.8 kDa. GDF5 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDF5 solution contains 10mM sodium citrate pH-3.5 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GDF-5 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.
Synonyms
Cartilage-derived morphogenetic protein-1, CDMP-1, LAP4, SYNS2, GDF-5, Radotermin, CDMP1, GDF5, Growth differentiation factor 5, BMP-14.
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 MAPLATRQGK RPSKNLKARC SRKALHVNFK DMGWDDWIIA PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ TLMNSMDPES TPPTCCVPTR LSPISILFID SANNVVYKQY EDMVVESCGC R.
Background
What is the molecular weight/Mw of GDF5 HUMAN, HIS Protein?
GDF5 HUMAN, HIS Protein has a total Mw of 15.8kDa.

What is the source or expression system of GDF5 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of GDF5 HUMAN, HIS Protein?
GDF5 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF5 HUMAN, HIS Protein?
The biological functionality of GDF5 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of GDF5 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MAPLATRQGK RPSKNLKARC SRKALHVNFK DMGWDDWIIA PLEYEAFHCE GLCEFPLRSH LEPTNHAVIQ TLMNSMDPES TPPTCCVPTR LSPISILFID SANNVVYKQY EDMVVESCGC R.

What applications can GDF5 HUMAN, HIS Protein be used in?
GDF5 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF5 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF5 HUMAN, HIS 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:

TP53 Regulated Inhibitor Of Apoptosis 1 Human Recombinant

TP53 Regulated Inhibitor of Apoptosis 1, P53-Inducible Cell-Survival Factor, Mitochondrial Distribution And Morphology 35 Homolog, Protein 15E1.1, MDM35, WF-1, p53CSV, HSPC132.

Product # :

PRO-1771

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Description

TRIAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 99 amino acids (1-76 a.a) and having a molecular mass of 11.2kDa.TRIAP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TRIAP1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TRIAP1 has a p53-binding site in its second exon. TRIAP1 expression is reduced by small interfering RNA enhanced apoptosis, while overexpression of TRIAP1 protects cells from apoptosis triggered by DNA damage. TRIAP1 is highly induced when cells have low levels of genotoxic stresses, but not when DNA damage is severe. TRIAP1 is able to control apoptotic pathways by interacting with Hsp70 which inhibits activity of apoptosis protease activating factor-1.
Synonyms
TP53 Regulated Inhibitor of Apoptosis 1, P53-Inducible Cell-Survival Factor, Mitochondrial Distribution And Morphology 35 Homolog, Protein 15E1.1, MDM35, WF-1, p53CSV, HSPC132.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNSVGEA CTDMKREYDQ CFNRWFAEKF LKGDSSGDPC TDLFKRYQQC VQKAIKEKEI PIEGLEFMGH GKEKPENSS

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:

Macrophage Migration Inhibitory Factor Rat Recombinant

Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

Product # :

CYT-193

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Description

MIF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa. The MIF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.

Purity

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

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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
Synonyms
Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF 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 MIF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTSDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.

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 Receptor-1B Human Recombinant

Bone Morphogenetic Protein Receptor, Type IB, BMP Type-1B Receptor, EC 2.7.11.30, BMPR-1B, ALK6, Bone Morphogenetic Protein Receptor Type-1B, Serine/Threonine Receptor Kinase, CDw293 Antigen, EC 2.7.11, CDw293, ALK-6, Bone morphogenetic protein receptor type-1B.

Product # :

CYT-897

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Description

BMPR1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (14-126 a.a) and having a molecular mass of 15.1kDa. BMPR1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMPR1B protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Bone Morphogenetic protein Receptor-1B, also known as BMPR1B belongs to the TKL Ser/Thr protein kinase family. BMPR1Bis on ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate as well as activate type I receptors which autophosphorylate, afterward bind and activate SMAD transcriptional regulators. BMPR1B is receptor for BMP7/OP-1 as well as GDF5.
Synonyms
Bone Morphogenetic Protein Receptor, Type IB, BMP Type-1B Receptor, EC 2.7.11.30, BMPR-1B, ALK6, Bone Morphogenetic Protein Receptor Type-1B, Serine/Threonine Receptor Kinase, CDw293 Antigen, EC 2.7.11, CDw293, ALK-6, Bone morphogenetic protein receptor type-1B.
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 MGSKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD GPIHHR.
Background
Bone Morphogenetic Protein Receptor-1B Human Recombinant: A Key Regulator of Cellular Signaling in Development and Disease
Abstract:
Bone Morphogenetic Protein Receptor-1B (BMPR1B) human recombinant is a critical component of the bone morphogenetic protein (BMP) signaling pathway, governing cellular processes such as embryogenesis, tissue homeostasis, and disease progression. This research paper provides a comprehensive analysis of BMPR1B, including its characteristics, signaling mechanisms, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMPR1B human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
The precise regulation of cellular signaling pathways is essential for proper development and tissue maintenance. BMPR1B, a key receptor in the BMP pathway, plays a crucial role in various biological processes. This paper explores the unique features of BMPR1B and presents novel approaches for its production and optimization, aiming to unravel its therapeutic potential in a wide range of developmental and disease contexts.
Characteristics and Signaling Mechanisms:
BMPR1B belongs to the serine/threonine kinase receptor family and is predominantly expressed in embryonic tissues, skeletal structures, and reproductive organs. Upon binding to BMP ligands, BMPR1B initiates downstream signaling cascades, including Smad-dependent and Smad-independent pathways. These pathways regulate gene expression, cellular proliferation, differentiation, and apoptosis, ultimately influencing tissue development and homeostasis.
Production of BMPR1B Human Recombinant:
Efficient production methodologies are pivotal for harnessing the therapeutic potential of BMPR1B human recombinant. Mammalian expression systems, such as Chinese hamster ovary (CHO) cells, have been widely employed to ensure proper folding and post-translational modifications of the receptor. Optimization strategies, including codon optimization and vector engineering, have been utilized to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to obtain high-quality BMPR1B recombinant protein.
Potential Therapeutic Applications:
BMPR1B human recombinant holds tremendous promise in the field of regenerative medicine and disease therapy. Dysregulation of the BMP signaling pathway has been implicated in various developmental disorders, including skeletal abnormalities and congenital malformations. Modulating BMPR1B activity using BMPR1B human recombinant may offer a targeted approach for promoting tissue regeneration and repair in these conditions. Furthermore, BMPR1B signaling is involved in several diseases, such as cancer and cardiovascular disorders, highlighting its potential as a therapeutic target for intervention.
Conclusion:
BMPR1B human recombinant represents a vital regulator in cellular signaling, with significant implications in development and disease. Optimizing production methodologies and expanding our understanding of its signaling mechanisms will further enhance its therapeutic potential. With its involvement in various biological processes and disease contexts, BMPR1B human recombinant emerges as a promising tool for regenerative medicine and targeted therapeutics.
What is the molecular weight/Mw of BMPR1B Protein?
BMPR1B Protein has a total Mw of 15.1kDa.

What is the source or expression system of BMPR1B Protein?
Escherichia Coli.

What is the Purity of BMPR1B Protein?
BMPR1B Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of BMPR1B Protein?
The biological functionality of BMPR1B Protein will be determined in the future.

What is the amino acid sequence of BMPR1B Protein?
MGSSHHHHHH SSGLVPRGSH MGSKKEDGES TAPTPRPKVL RCKCHHHCPE DSVNNICSTD GYCFTMIEED DSGLPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKNRDFVD GPIHHR.

What applications can BMPR1B Protein be used in?
BMPR1B Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMPR1B Protein?
The endotoxin level is minimal, BMPR1B 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:

AITR Human Recombinant

TNFRSF18, AITR, CD357, GITR, GITR-D, Tumor necrosis factor receptor superfamily member 18, Activation-inducible TNFR family receptor, Glucocorticoid-induced TNFR-related protein, CD357, UNQ319/PRO364.

Product # :

CYT-925

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Description

AITR Human Recombinant produced in Sf9 Baculovirus is a single, glycosylated polypeptide chain containing 145 amino acids (26-162a.a.) and having a molecular mass of 15.6kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).AITR is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AITR protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

sds-page

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Synonyms
TNFRSF18, AITR, CD357, GITR, GITR-D, Tumor necrosis factor receptor superfamily member 18, Activation-inducible TNFR family receptor, Glucocorticoid-induced TNFR-related protein, CD357, UNQ319/PRO364.
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
QRPTGGPGCG PGRLLLGTGT DARCCRVHTT RCCRDYPGEE CCSEWDCMCV QPEFHCGDPC CTTCRHHPCP PGQGVQSQGK FSFGFQCIDC ASGTFSGGHE GHCKPWTDCT QFGFLTVFPG NKTHNAVCVP GSPPAEPLEH HHHHH.
Background
AITR Human Recombinant: Unveiling its Role in Immune Regulation and Therapeutic Potential
1. Abstract
This research paper aims to provide a comprehensive exploration of the AITR Human Recombinant, a crucial receptor involved in immune regulation. By examining its structure, signaling pathways, biological functions, and implications in disease, we unravel the potential therapeutic applications of AITR in immune-related disorders.
2. Introduction
AITR, also known as TNFRSF18, is a receptor protein that plays a vital role in immune regulation. With its involvement in T-cell responses and immune tolerance, AITR has emerged as an intriguing target for therapeutic interventions in various immune-mediated conditions.
3. Structure and Signaling of AITR
AITR is a transmembrane receptor protein belonging to the tumor necrosis factor receptor superfamily. Its extracellular domain interacts with its ligand, glucocorticoid-induced TNFR-related protein (GITR) ligand, leading to downstream signaling events that modulate immune cell function.
4. Biological Functions of AITR
AITR activation influences T-cell responses by regulating T-cell activation, proliferation, and cytokine production. Additionally, AITR signaling can modulate the balance between effector and regulatory T-cell populations, thereby playing a role in immune tolerance and immune homeostasis.
5. AITR in Disease Pathology
AITR dysregulation has been associated with various immune-related disorders, including autoimmune diseases, cancer, and transplant rejection. Understanding the role of AITR in these pathologies may provide insights into potential therapeutic strategies targeting AITR signaling.
6. Therapeutic Potential of AITR
The unique role of AITR in immune regulation makes it an appealing target for therapeutic interventions. Modulation of AITR signaling holds promise for manipulating immune responses in the context of autoimmune diseases, cancer immunotherapy, and transplantation.
7. Conclusion and Future Perspectives
While our understanding of AITR and its functions has advanced significantly, further research is warranted to unravel its complex signaling pathways and therapeutic potential. Continued investigations into AITR biology will enhance our ability to develop targeted therapies for immune-related disorders.
What is the molecular weight/Mw of AITR Protein?
AITR Protein has a total Mw of 15.6kDa.

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

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

What is the Biological Activity of AITR Protein?
The biological functionality of AITR Protein will be determined in the future.

What is the amino acid sequence of AITR Protein?
QRPTGGPGCG PGRLLLGTGT DARCCRVHTT RCCRDYPGEE CCSEWDCMCV QPEFHCGDPC CTTCRHHPCP PGQGVQSQGK FSFGFQCIDC ASGTFSGGHE GHCKPWTDCT QFGFLTVFPG NKTHNAVCVP GSPPAEPLEH HHHHH.

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

What is the endotoxin level for AITR Protein?
The endotoxin level is minimal, AITR 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:

TRAF-Interacting Protein with Forkhead-Associated Domain Human Recombinant

TRAF-interacting protein with FHA domain-containing protein A, Putative MAPK-activating protein PM14, Putative NF-kappa-B-activating protein 20, TRAF2-binding protein, TIFA, T2BP, T6BP, TIFAA.

Product # :

PRO-1041

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Description

TIFA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-184 a.a.) and having a molecular mass of 24kDa.TIFA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TRAF-interacting protein with FHA domain-containing protein A (TIFA) is an adapter protein that mediates the IRAK1 and TRAF6 interaction following IL-1 stimulation, triggering the downstream activation of NF-kappa-B and AP-1 pathways. The TIFA protein stimulates the oligomerization and polyubiquitination of TRAF6, leading to the activation of TAK1 and IKK through a proteasome-independent mechanism.
Synonyms
TRAF-interacting protein with FHA domain-containing protein A, Putative MAPK-activating protein PM14, Putative NF-kappa-B-activating protein 20, TRAF2-binding protein, TIFA, T2BP, T6BP, TIFAA.
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 MGSHMTSFED ADTEETVTCL QMTVYHPGQL QCGIFQSISF NREKLPSSEV VKFGRNSNIC HYTFQDKQVS RVQFSLQLFK KFNSSVLSFE IKNMSKKTNL IVDSRELGYL NKMDLPYRCM VRFGEYQFLM EKEDGESLEF FETQFILSPR SLLQENNWPP HRPIPEYGTY SLCSSQSSSP TEMDENES.

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:

Histone Acetyltransferase 1 Human Recombinant

EC 2.3.1.48, KAT1, histone acety ltransferase 1, Histone acetyltransferase type B catalytic subunit, HAT1.

Product # :

ENZ-504

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Description

HAT1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (20-341 a.a.) and having a molecular mass of 40.1 kDa. The HAT1 is fused to a 21 amino acid His Tag and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HAT1 solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
HAT1 is a type B histone acetyltransferase that participates in the rapid acetylation of newly synthesized cytoplasmic histones, which are in turn imported into the nucleus for de novo deposition onto nascent DNA chains. Histone acetylation, mainly of soluble histone H4 at ''Lys-5'' and ''Lys-12'' and acetylates histone H2A at ''Lys-5''. HAT1 takes part in replication-dependent chromatin assembly. HAT1 acetylates soluble but not nucleosomal histone H4 at lysines 5 and 12, and to a lesser degree, histone H2A at lysine 5. HAT1 has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG.
Synonyms
EC 2.3.1.48, KAT1, histone acety ltransferase 1, Histone acetyltransferase type B catalytic subunit, HAT1.
Physical Appearance
Sterile Filtered clear 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 MKKLAEYKCN TNTAIELKLV RFPEDLENDI RTFFPEYTHQ LFGDDETAFG YKGLKILLYY IAGSLSTMFR VEYASKVDEN FDCVEADDVE GKIRQIIPPG FCTNTNDFLS LLEKEVDFKP FGTLLHTYSV LSPTGGENFT FQIYKADMTC RGFREYHERL QTFLMWFIET ASFIDVDDER WHYFLVFEKY NKDGATLFAT VGYMTVYNYY VYPDKTRPRV SQMLILTPFQ GQGHGAQLLE TVHRYYTEFP TVLDITAEDP SKSYVKLRDF VLVKLCQDLP CFSREKLMQG FNEDMAIEAQ QKFKINKQHA RRVYEILRLL VTD.

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:

TNFAIP3 Interacting Protein 1 Human Recombinant

TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-1.

Product # :

PRO-005

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Description

TNIP1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 458 amino acids (94-530 a.a.) and having a molecular mass of 51.8kDa. The TNIP1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TNIP1 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 20% glycerol, 5mM DTT and 200mM NaCl.

Purity

Greater than 75.0% as determined by SDS-PAGE.

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Introduction
TNFAIP3-interacting protein 1 (TNIP1) interacts with zinc finger protein A20/TNFAIP3 and inhibits TNF-induced NF-kappa-B-dependent gene expression by interfering with a RIP- or TRAF2-mediated transactivation signal. Furthermore, TNIP1 interacts with HIV-1 matrix protein and is packaged into virions and its overexpression can inhibit viral replication. TNIP1 can regulate matrix nuclear localization, both nuclear import of Preintegration complex (PIC) and export of GAG polyprotein and viral genomic RNA during virion production.
Synonyms
TNFAIP3-interacting protein 1, HIV-1 Nef-interacting protein, Nef-associated factor 1, Naf1, Nip40-1, Virion-associated nuclear shuttling protein, VAN, hVAN, TNIP1, KIAA0113, NAF1, ABIN-1.
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 MSNVTASPTA PACPSDKPAP VQKPPSSGTS SEFEVVTPEE QNSPESSSHA NAMALGPLPR EDGNLMLHLQ RLETTLSVCA EEPDHGQLFT HLGRMALEFN RLASKVHKNE QRTSILQTLC EQLRKENEAL KAKLDKGLEQ RDQAAERLRE ENLELKKLLM SNGNKEGASG RPGSPKMEGT GKKAVAGQQQ ASVTAGKVPE VVALGAAEKK VKMLEQQRSE LLEVNKQWDQ HFRSMKQQYE QKITELRQKL ADLQKQVTDL EAEREQKQRD FDRKLLLAKS KIEMEETDKE QLTAEAKELR QKVKYLQDQL SPLTRQREYQ EKEIQRLNKA LEEALSIQTP PSSPPTAFGS PEGAGALLRK QELVTQNELL KQQVKIFEED FQRERSDRER MNEEKEELKK QVEKLQAQVT LSNAQLKAFK DEEKAREALR QQKRKAKA.

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:

Regulatory Factor X-Associated Ankyrin-Containing Protein Human Recombinant

ANKRA1, BLS, F14150_1, RFX-B, DNA-binding protein RFXANK, Ankyrin repeat family A protein 1, Regulatory factor X subunit B, Regulatory factor X-associated ankyrin-containing protein, RFXANK, RFXB.

Product # :

PRO-1537

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Description

RFXANK Human Recombinant produced in E. coli is a single polypeptide chain containing 260 amino acids (1-237) and having a molecular mass of 28kDa. RFXANK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RFXANK solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Regulatory Factor X-Associated Ankyrin-Containing Protein (RFXANK) contains ankyrin repeats involved in protein-protein interactions. RFXANK, along with regulatory factor X-associated protein and regulatory factor-5, figures a complex which binds to the X box motif of certain MHC class II gene promoters and activates their transcription. After bound to the promoter, this complex associates with the non-DNA-binding factor MHC class II transactivator, which controls the cell type specificity and inducibility of MHC class II gene expression. Mutations in RFXANK have been linked to bare lymphocyte syndrome type II, complementation group B.
Synonyms
ANKRA1, BLS, F14150_1, RFX-B, DNA-binding protein RFXANK, Ankyrin repeat family A protein 1, Regulatory factor X subunit B, Regulatory factor X-associated ankyrin-containing protein, RFXANK, RFXB.
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 MGSMELTQPA EDLIQTQQTP ASELGDPEDP GEEAADGSDT VVLSLFPCTP EPVNPEPDAS VSSPQGSSLK HSTTLTNRQR GNEVSALPAT LDCDNLVNKP DERGFTPLIW ASAFGEIETV RFLLEWGADP HILAKERESA LSLASTGGYT DIVGLLLERD VDINIYDWNG GTPLLYAVRG NHVKCVEALL ARGADLTTEA DSGYTPMDLA VALGYRKVQQ VIENHILKLF QSNLVPADPE.

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.

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