Search: 1000 results found for "activating transcription factor"

Description:

MOB1, Mps One Binder kinase Activator-Like 3 Human Recombinant

Mps one binder kinase activator-like 3, 2C4D, Class II mMOB1, Mob1 homolog 3, Mob3, Preimplantation protein 3, MOBKL3, MOB3, PREI3, MOB1, PREI3, CGI-95, MGC12264.

Product # :

PRO-049

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Description

MOBKL3 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 245 amino acids (1-225 a.a.) and having a molecular mass of 28.1kDa. The MOBKL3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MOBKL3 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) containing 0.2M Nacl, 5mM DTT, 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Mps one binder kinase activator-like 3 (MOBKL3) is a member of the MOB1/Phocein family and is phosphorylated on serine residues. MOBKL3 is usually linked with membranes but can be present in the cytosol, where it behaves as a protein complex. MOBKL3 is the major partner of the striatin family members, which are scaffolding proteins involved in signaling and trafficking.
Synonyms
Mps one binder kinase activator-like 3, 2C4D, Class II mMOB1, Mob1 homolog 3, Mob3, Preimplantation protein 3, MOBKL3, MOB3, PREI3, MOB1, PREI3, CGI-95, MGC12264.
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 MVMAEGTAVL RRNRPGTKAQ DFYNWPDESF DEMDSTLAVQ QYIQQNIRAD CSNIDKILEP PEGQDEGVWK YEHLRQFCLE LNGLAVKLQS ECHPDTCTQM TATEQWIFLC AAHKTPKECP AIDYTRHTLD GAACLLNSNK YFPSRVSIKE SSVAKLGSVC RRIYRIFSHA YFHHRQIFDE YENETFLCHR FTKFVMKYNL MSKDNLIVPI LEEEVQNSVS GESEA.

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:

Myostatin Propeptide Human Recombinant

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Product # :

CYT-448

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Description

Recombinant Human Myostatin Propeptide is a 27.8kDa protein containing 244 amino acid residues of the human Myostatin Propeptide.

Source

Escherichia Coli.

Formulation

Lyophilized with no additives.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The protein has full biological activity when compared to a standard. The activity is determined by its ability to inhibit 50ng/ml of Myostatin on MPC-11 cells and is typically 0.13-0.2 μg/ml.

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Introduction
Myostatin (GDF-8), a member of the TGFbeta superfamily, is a potent and specific negative regulator of skeletal muscle mass. In serum, myostatin circulates as part of a latent complex containing myostatin propeptide and/or follistatin-related gene. The myostatin propeptide is known to bind and inhibit myostatin in vitro. This interaction is relevant in vivo, with a majority (>70%) of myostatin in serum bound to its propeptide. The myostatin propeptide is negative regulator of myostatin in vivo.
Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Physical Appearance
Sterile Filtered white lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
Solubility
It is recommended to reconstitute the lyophilized Myostatin Propeptide in sterile 20mM HCl at 0.1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MNENSEQKE NVEKEGLCNA CTWRQNTKSS RIEAIKIQIL SKLRLETAPN ISKDVIRQLL PKAPPLRELI DQYDVQRDDS SDGSLEDDDY HATTETIITM PTESDFLMQV DGKPKCCFFK FSSKIQYNKV VKAQLWIYLR PVETPTTVFV QILRLIKPMK DGTRYTGIRS LKLDMNPGTG IWQSIDVKTV LQNWLKQPES NLGIEIKALD ENGHDLAVTF PGPGEDGLNP FLEVKVTDTP KRSRR.

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:

Interleukin-1 alpha Rat Recombinant, His Tag Active

Interleukin-1 alpha, IL-1 alpha.

Product # :

CYT-1100

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Description

IL1A Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (115-270 a.a) and having a molecular mass of 20.2kDa.IL1A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

IL1A protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

The ED50 that was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell is <20 pg/ml.

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Introduction
IL-1 alpha is produced by activated macrophages.IL-1 alpha stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins take part in the inflammatory response, being identified as endogenous pyrogens, and stimulate the release of prostaglandin and collagenase from synovial cells.
Synonyms
Interleukin-1 alpha, IL-1 alpha.
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 MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD
RIHLKAASLN DLQLEVKFDM YAYSSGGDDSKYPVTLKVSN TQLFVSAQGE DKPVLLKEIP
ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.
Background
What is the molecular weight/Mw of IL1A RAT, HIS ACTIVE Protein?
IL1A RAT, HIS ACTIVE Protein has a total Mw of 20.2kDa.

What is the source or expression system of IL1A RAT, HIS ACTIVE Protein?
Escherichia Coli.

What is the Purity of IL1A RAT, HIS ACTIVE Protein?
IL1A RAT, HIS ACTIVE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IL1A RAT, HIS ACTIVE Protein?
The ED50 that was measured in a cell proliferation assay using D10.G4.1 mouse helper T cell is <20 pg/ml.

What is the amino acid sequence of IL1A RAT, HIS ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD
RIHLKAASLN DLQLEVKFDM YAYSSGGDDSKYPVTLKVSN TQLFVSAQGE DKPVLLKEIP
ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.
.What applications can IL1A RAT, HIS ACTIVE Protein be used in?
IL1A RAT, HIS ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL1A RAT, HIS ACTIVE Protein?
The endotoxin level is minimal, IL1A RAT, HIS ACTIVE 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:

Stromal Cell-Derived Factor-1 alpha Rat Recombinant (CXCL12)

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, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

Product # :

CHM-354

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Description

Stromal Cell-Derived Factor-1 alpha Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 7.9 kDa. The SDF-1a is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CXCL12 protein was lyophilized from a concentrated (1 mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 150mM NaCl.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 50-100 ng/ml.

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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, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SDF-1a 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 reconstitute the lyophilized SDF-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNK.
Background
What is the molecular weight/Mw of CXCL12 RAT ALPHA Protein?
CXCL12 RAT ALPHA Protein has a total Mw of 7.9kDa.

What is the source or expression system of CXCL12 RAT ALPHA Protein?
Escherichia Coli.

What is the Purity of CXCL12 RAT ALPHA Protein?
CXCL12 RAT ALPHA Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL12 RAT ALPHA Protein?
The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 50-100ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

What is the amino acid sequence of CXCL12 RAT ALPHA Protein?
KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNK.

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

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

Who supplies recombinant CXCL12 RAT ALPHA 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 RAT ALPHA?
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:

Monocyte Chemotactic Protein-1 Rat Recombinant, Sf9

Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11

Product # :

CHM-044

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Description

MCP1 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148 aa) and having a molecular mass of 15.1kDa.MCP1 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells

Formulation

The MCP1 Rat protein solution (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belongs to the CC chemokine family which is also known as monocyte chemotactic protein-1 (MCP-1). MCP 1 is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts. CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. MCP 1is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.
Synonyms
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11
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
ADPQPDAVNA PLTCCYSFTG KMIPMSRLEN YKRITSSRCP KEAVVFVTKL KREICADPNK EWVQKYIRKL DQNQVRSETT VFYKIASTLR TSAPLNVNLT HKSEANASTL FSTTTSSTSV EVTSMTENHH HHHH
Background
What is the molecular weight/Mw of CCL2 RAT, SF9 Protein?
CCL2 RAT, SF9 Protein has a total Mw of 15.1kDa.

What is the source or expression system of CCL2 RAT, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of CCL2 RAT, SF9 Protein?
CCL2 RAT, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 RAT, SF9 Protein?
The biological functionality of CCL2 RAT, SF9 Protein will be determined in the future.

What is the amino acid sequence of CCL2 RAT, SF9 Protein?
ADPQPDAVNA PLTCCYSFTG KMIPMSRLEN YKRITSSRCP KEAVVFVTKL KREICADPNK EWVQKYIRKL DQNQVRSETT VFYKIASTLR TSAPLNVNLT HKSEANASTL FSTTTSSTSV EVTSMTENHH HHHH

What applications can CCL2 RAT, SF9 Protein be used in?
CCL2 RAT, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL2 RAT, SF9 Protein?
The endotoxin level is minimal, CCL2 RAT, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL2 RAT, SF9 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 CCL2 RAT, SF9?
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:

Osteoclast Stimulating Factor-1, Mouse Anti Human

SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

Product # :

ANT-056

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Formulation

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

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Introduction
OSTF1 is an intracellular protein produced by osteoclasts that induces bone resorption, via signaling cascade which results in the secretion of factors enhancing osteoclast formation and activity.
Synonyms
SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.
Immunogen
Anti-human OSTF1 mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human OSTF1 amino acids 1-217 purified from E. coli.
Ig Subclass
Mouse IgG2a heavy chain and k light chain.
Clone
PAT9G4AT.
Applications
OSTF1 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF 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
OSTF1 antibody was purified from mouse ascitic fluids by protein-G 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:

Growth Arrest and DNA-Damage-Inducible Gamma Interacting Protein 1 Human Recombinant

Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.

Product # :

PRO-972

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Description

GADD45GIP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (48-222) and having a molecular mass of 22.6 kDa.GADD45GIP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GADD45GIP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2M NaCl and 40% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
GADD45GIP1 is a nuclear protein which takes part in apoptosis control. GADD45GIP1 is expressed in several tissues, such as heart, thyroid, trachea, kidney, ovary, pancreas, testis and stomach and acts as a negative regulator of G1 to S phase cell cycle production by collaborating with GADD45 proteins to inhibit the activity of cyclin-dependent kinases.
Synonyms
Growth arrest and DNA-damage-inducible gamma interacting protein 1, PRG6, CRIF1, PLINP-1, KBBP2, Plinp1, Papillomavirus L2-interacting nuclear protein 1, CKII beta-associating protein, CR6-interacting factor 1, p53-responsive gene 6 protein, CKII beta binding protein 2, growth arrest and DNA damage-inducible proteins-interacting protein 1, papillomavirus L2 interacting nuclear protein 1, PLINP1.
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 MPRWQLGPRY AAKQFARYGA ASGVVPGSLW PSPEQLRELE AEEREWYPSL ATMQESLRVK QLAEEQKRRE REQHIAECMA KMPQMIVNWQ QQQRENWEKA QADKERRARL QAEAQELLGY QVDPRSARFQ ELLQDLEKKE RKRLKEEKQK RKKEARAAAL AAAVAQDPAA SGAPSS

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:

Thymidine Kinase 1 Human Recombinant

Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

Product # :

PKA-036

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Description

TK1 Human Recombinant produced in E. coli is a single polypeptide chain containing 258 amino acids (1-234) and having a molecular mass of 28.0 kDa.TK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TK1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.
Synonyms
Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.
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 MGSHMSCINL PTVLPGSPSK TRGQIQVILG PMFSGKSTEL MRRVRRFQIA QYKCLVIKYA KDTRYSSSFC THDRNTMEAL PACLLRDVAQ EALGVAVIGI DEGQFFPDIV EFCEAMANAG KTVIVAALDG TFQRKPFGAI LNLVPLAESV VKLTAVCMEC FREAAYTKRL GTEKEVEVIG GADKYHSVCR LCYFKKASGQ PAGPDNKENC PVPGKPGEAV AARKLFAPQQ ILQCSPAN.

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 Mouse Recombinant

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

Product # :

PKA-139

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Description

FLT1 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (23-759 a.a) containing a total of 970 amino acids, having a molecular mass of 108.9kDa. FLT1 is fused to a 233 amino acid hIgG-his tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK 293.

Formulation

FLT1 protein solution (1mg/ml) containing 10% glycerol and PBS.

Purity

Greater than 85.0% as determined by SDS-PAGE.

Biological Activity

The ED50 range ≤ 50ng/ml and is measured by its ability to inhibit proliferation using HUVEC human umbilical vein endothelial cells in the presence of Human VEGF165.

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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 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
YGSGSKLKVP ELSLKGTQHV MQAGQTLFLK CRGEAAHSWS LPTTVSQEDK RLSITPPSAC GRDNRQFCST LTLDTAQANH TGLYTCRYLP TSTSKKKKAE SSIYIFVSDA GSPFIEMHTD IPKLVHMTEG RQLIIPCRVT SPNVTVTLKK FPFDTLTPDG QRITWDSRRG FIIANATYKE IGLLNCEATV NGHLYQTNYL THRQTNTILD VQIRPPSPVR LLHGQTLVLN CTATTELNTR VQMSWNYPGK ATKRASIRQR IDRSHSHNNV FHSVLKINNV ESRDKGLYTC RVKSGSSFQS FNTSVHVYEK GFISVKHRKQ PVQETTAGRR SYRLSMKVKA FPSPEIVWLK DGSPATLKSA RYLVHGYSLI IKDVTTEDAG DYTILLGIKQ SRLFKNLTAT LIVNVKPQIY EKSVSSLPSP PLYPLGSRQV LTCTVYGIPR PTITWLWHPC HHNHSKERYD FCTENEESFI LDPSSNLGNR IESISQRMTV IEGTNKTVST LVVADSQTPG IYSCRAFNKI GTVERNIKFY VTDVPNGFHV SLEKMPAEGE DLKLSCVVNK FLYRDITWIL LRTVNNRTMH HSISKQKMAT TQDYSITLNL VIKNVSLEDS GTYACRARNI YTGEDILRKT EVLVRDSEAP HLLQNLSDYE VSISGSTTLD CQARGVPAPQ ITWFKNNHKI QQEPGIILGP GNSTLFIERV TEEDEGVYRC RATNQKGAVE
Background
Endothelial cells express 3 different vascular endothelial growth factor receptors: VEGFR-1 (Flt1), VEGFR-2 (KDR/Flk1), VEGFR-3 (Flt4) which are a part of the receptor tyrosine kinases family. Those receptors express mostly in endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. Flt1 contains 7 immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Flt-1, when compared to VEGFR-2 receptor has a higher affinity for VEGF but a weaker signalling activity. VEGFR-1 also mediates signals for differentiation.

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:

Interleukin-3 Rhesus Macaque Recombinant

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399

Product # :

CYT-156

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Description

IL 3 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a molecular mass of 14.0kDa.The IL 3 Rhesus Macaque is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of the proliferation of human
TF-1 cells is less than 0.1ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-3 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 IL-3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APMTQTTSLK TSWAKCSNMI DEIITHLNQP PLPSPDFNNL NEEDQTILVE KNLRRSNLEA FSKAVKSLQN ASAIESILKN LPPCLPMATA APTRPPIRIT NGDRNDFRRK LKFYLKTLEN EQAQ
Background
What is the molecular weight/Mw of IL 3 RHESUS MACAQUE Protein?
IL 3 RHESUS MACAQUE Protein has a total Mw of 14kDa.

What is the source or expression system of IL 3 RHESUS MACAQUE Protein?
Escherichia Coli.

What is the Purity of IL 3 RHESUS MACAQUE Protein?
IL 3 RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 RHESUS MACAQUE Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells is less than 0.1ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of IL 3 RHESUS MACAQUE Protein?
APMTQTTSLK TSWAKCSNMI DEIITHLNQP PLPSPDFNNL NEEDQTILVE KNLRRSNLEA FSKAVKSLQN ASAIESILKN LPPCLPMATA APTRPPIRIT NGDRNDFRRK LKFYLKTLEN EQAQ.

What applications can IL 3 RHESUS MACAQUE Protein be used in?
IL 3 RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 3 RHESUS MACAQUE Protein?
The endotoxin level is minimal, IL 3 RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 3 RHESUS MACAQUE 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 IL 3 RHESUS MACAQUE?
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:

CD30 Human Recombinant

CD30, D1S166E, KI-1, Tumor necrosis factor receptor superfamily member 8, CD30L receptor, Ki-1 antigen, Lymphocyte activation antigen CD30, TNFRSF8.

Product # :

PRO-1369

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Description

CD30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (19-379a.a.) and having a molecular mass of 40.8kDa. CD30 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

CD30 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Tumor necrosis factor receptor superfamily member 8 (CD30) is a member of the TNF-receptor superfamily. CD30 is expressed by activated (not by resting) T and B cells. CD30 interacts with TRAF2 and TRAF5 which mediate the signal transduction that leads to the activation of NF-kappaB. CD30 is a positive regulator of apoptosis, and also has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity.
Synonyms
CD30, D1S166E, KI-1, Tumor necrosis factor receptor superfamily member 8, CD30L receptor, Ki-1 antigen, Lymphocyte activation antigen CD30, TNFRSF8.
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 MGSFPQDRPF EDTCHGNPSH YYDKAVRRCC YRCPMGLFPT QQCPQRPTDC RKQCEPDYYL DEADRCTACV TCSRDDLVEK TPCAWNSSRV CECRPGMFCS TSAVNSCARC FFHSVCPAGM IVKFPGTAQK NTVCEPASPG VSPACASPEN CKEPSSGTIP QAKPTPVSPA TSSASTMPVR GGTRLAQEAA SKLTRAPDSP SSVGRPSSDP GLSPTQPCPE GSGDCRKQCE PDYYLDEAGR CTACVSCSRD DLVEKTPCAW NSSRTCECRP GMICATSATN SCARCVPYPI CAAETVTKPQ DMAEKDTTFE APPLGTQPDC NPTPENGEAP ASTSPTQSLL VDSQASKTLP IPTSAPVALS STGK.

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:

Proteasome Activator Subunit 1 Human Recombinant

REG-alpha, PA28alpha, PA28a, Proteasome Activator subunit-1, Proteasome Activator 28 subunit alpha.

Product # :

PRO-266

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Description

PSME1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-249a.a.) and having a molecular mass of 30.8kDa.PSME1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PSME1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
PSME1 is a Proteasome Activator 28 subunit alpha essential for presentation of certain major histocompatibility (MHC) class I antigens. The PSME1 complex is an alternate proteasome activator which operates with no use of ubiquitin. The PSME1 complex is made out of two homologous subunits, alpha and beta, that functions in similar catalytic properties and is connected to a hexameric ring.
Synonyms
REG-alpha, PA28alpha, PA28a, Proteasome Activator subunit-1, Proteasome Activator 28 subunit alpha.
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.Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAMLRVQPEA QAKVDVFRED LCTKTENLLG SYFPKKISEL DAFLKEPALN EANLSNLKAP LDIPVPDPVK EKEKEERKKQ QEKEDKDEKK KGEDEDKGPP CGPVNCNEKI VVLLQRLKPE IKDVIEQLNL VTTWLQLQIP RIEDGNNFGV AVQEKVFELM TSLHTKLEGF HTQISKYFSE RGDAVTKAAK QPHVGDYRQL VHELDEAEYR DIRLMVMEIR NAYAVLYDII LKNFEKLKKP RGETKGMIY

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-CC Human Recombinant

Platelet Derived Growth Factor C, Spinal Cord-Derived Growth Factor, FALLOTEIN, PDGF-C, VEGF-E, SCDGF, Secretory Growth Factor-Like Protein, Platelet-Derived Growth Factor C, PDGFC.

Product # :

CYT-872

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Description

PDGF-CC Human Recombinant (235-345) produced in E.Coli is a disulfide-linked homodimer containing 2x118 amino acids and having a total molecular mass of 26.8kDa.The PDGF-CC is fused to a 7 amino acid His tag [M-HHHHHH] at N-terminal and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as measured in a proliferation assay using mouse NR6R-3T3 cells, is less than 350ng/ml.

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Introduction
Platelet Derived Growth Factor-CC (PDGF-CC) belongs to the PGDF family of growth factors. PDGF-CC binds with high-affinity to PDGF R-a and activates PDGF R-ab heterodimers. During development, PDGF-CC is involved in ductal morphogenesis, cardiovascular smooth muscle cell proliferation; also PDGF-CC is an angiogenic factor. Furthermore, PDGF-CC is expressed in numerous tumors and tumor cell lines, and may be linked with tumorigenesis.
Synonyms
Platelet Derived Growth Factor C, Spinal Cord-Derived Growth Factor, FALLOTEIN, PDGF-C, VEGF-E, SCDGF, Secretory Growth Factor-Like Protein, Platelet-Derived Growth Factor C, PDGFC.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized PDGF-CC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-CC 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-CC in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MHHHHHHVVD LNLLTEEVRL YSCTPRNFSV SIREELKRTD TIFWPGCLLV KRCGGNCACC LHNCNECQCV PSKVTKKYHE VLQLRPKTGV RGLHKSLTDV ALEHHEECDC VCRGSTGG.

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:

Thrombopoietin Mouse Recombinant

Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.

Product # :

CYT-346

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Quantity :

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Shipped at Room temp

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Description

Thrombopoietin Mouse Recombinant produced in E.Coli is a single, non-glycosylated soluble polypeptide chain containing 174 amino acids and having a molecular mass of 18704 Dalton. The TPO is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

ED₅₀ range is less than 0.8ng/ml as determined by the dose dependent stimulation of Mo7e cells.

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Introduction
Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidneyt hat regulates the production of platelets by the bone marrow. It stimulates the production and differentiation of megakaryocytes, the bone marrow cells that fragment into large numbers of platelets.
Synonyms
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thrombopoietin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TPO Mouse 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 Thrombopoietin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPVAPACDPR LLNKLLRDSH LLHSRLSQCP DVDPLSIPVL LPAVDFSLGE WKTQTEQSKA QDILGAVSLL LEGVMAARGQ LEPSCLSSLL GQLSGQVRLL LGALQGLLGT QLPLQGRTTA HKDPNALFLS LQQLLRGKVR FLLLVEGPTL CVRRTLPTTA VPSSTSQLLT LNKF.

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 Activation Protein Alpha Human Recombinant

Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, FAPalpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, Seprase, SIMP, FAP

Product # :

ENZ-1160

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Description

FAP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 744 amino acids (26-760aa) and having a molecular mass of 86.1 kDa.FAP is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The FAP solution (0.25mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity > 5,000 pmol/min/ug. It is defined by the amount of enzyme that hydrolyzes 1.0 pmole of ZGP-AMC per minute at pH 7.5, at 37˚C.

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Introduction
DPP4 also called adenosine deaminase complexing protein-2, and T-cell activation antigen CD26 is a serine exopeptidase and complex enzyme that is expressed on the surface of most cell types. DPPIV is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. DPP4 plays a role in t-cell activation. DPP4 is associated with intracellular signal transduction, apoptosis and involved in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and GLP-1.
Synonyms
Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, FAPalpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, Seprase, SIMP, FAP
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
ADPLRPSRVH NSEENTMRAL TLKDILNGTF SYKTFFPNWI SGQEYLHQSA DNNIVLYNIE TGQSYTILSN RTMKSVNASN YGLSPDRQFV YLESDYSKLW RYSYTATYYI YDLSNGEFVR GNELPRPIQY LCWSPVGSKL AYVYQNNIYL KQRPGDPPFQ ITFNGRENKI FNGIPDWVYE EEMLATKYAL WWSPNGKFLA YAEFNDTDIP VIAYSYYGDE QYPRTINIPY PKAGAKNPVV RIFIIDTTYP AYVGPQEVPV PAMIASSDYY FSWLTWVTDE RVCLQWLKRV QNVSVLSICD FREDWQTWDC PKTQEHIEES RTGWAGGFFV STPVFSYDAI SYYKIFSDKD GYKHIHYIKD TVENAIQITS GKWEAINIFR VTQDSLFYSS NEFEEYPGRR NIYRISIGSY PPSKKCVTCH LRKERCQYYT ASFSDYAKYY ALVCYGPGIP ISTLHDGRTD QEIKILEENK ELENALKNIQ LPKEEIKKLE VDEITLWYKM ILPPQFDRSK KYPLLIQVYG GPCSQSVRSV FAVNWISYLA SKEGMVIALV DGRGTAFQGD KLLYAVYRKL GVYEVEDQIT AVRKFIEMGF IDEKRIAIWG WSYGGYVSSL ALASGTGLFK CGIAVAPVSS WEYYASVYTE RFMGLPTKDD NLEHYKNSTV MARAEYFRNV DYLLIHGTAD DNVHFQNSAQ IAKALVNAQV DFQAMWYSDQ NHGLSGLSTN HLYTHMTHFL KQCFSLSDHH 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:

Keratinocyte Growth Factor Human Recombinant

HBGF-7, FGF7, FGF-7, KGF.

Product # :

CYT-219

Price :

Quantity :

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Shipped at Room temp

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Description

Keratinocyte Growth Factor-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 164 amino acids and having a molecular mass of 18995 Dalton.The FGF-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered solution in 20mM PB, pH 8.0, 1M NaCl.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity was determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing KGF receptors yielding an ED₅₀ <10ng/ml, corresponding to a Specific Activity of 1.0×10⁵ IU/mg.

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Introduction
KGF 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. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.
Synonyms
HBGF-7, FGF7, FGF-7, KGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Keratinocyte Growth Factor1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF7 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 Keratinocyte Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MCNDMTPEQM ATNVNCSSPE RHTRSYDYME GGDIRVRRLF CRTQWYLRID KRGKVKGTQE MKNNYNIMEI RTVAVGIVAI KGVESEFYLA MNKEGKLYAK KECNEDCNFK ELILENHYNT YASAKWTHNG GEMFVALNQK GIPVRGKKTK KEQKTAHFLP MAIT.
Background
FGF stands for fibroblast growth factor that have proteins encoded inside them. The FGF family possess broad mitogenetic activities and are involved in a lot of processes in the body. Some of the biological processes that they are included in are embryonic development, cell growth, tumor growth and tissue repair. FGF-7 is often also commonly referred to as keratinocyte growth factor or KGF and studies have focused on the link between the protein and certain tumor growth.
Structure
Studies have found that the crystal structure of FGF7 is comparatively similar to that of FGF10. For instance, FGF7 does interact with D2, linker as well as D3 of the receptor. Similar to other FGFs much of interaction to do with D2 is confined to conserved residues as well as the residue Arg 251 in the linker domain and the hydrophobic surface of D2. That said there are notable differences and some models predict that FGF7 actually interacts with three loops in D3.
Mechanism
A member of the FGF family, this factor acts completely exclusively through a subset of FGF receptor isoforms. These are mainly expressed by epithelial cells. Indeed, studies suggest that the factor specifically acts on epithelial cells. This in turn causes increased proliferation differentiation and migrations of the aforementioned cells.
Interactions
FGF7 and FGF10 can interact with one of the FGF receptors that is expressed by the epithelial cells. As such, it could be the case that this interaction could cause a protective factor for these epithelial tissues. The protein has also been shown to interact with Perlecan. Also referred to as basement membrane specific heparan sulfate proteoglycan core protein, this is encoded by the HSPG2 gene. A large multi domain this cross-links and binds to various extracellular matrix components as well as self surface molecules. Since FGF7 binds specifically with the perlecan protein, research suggests that i should be considered a novel biological ligand for FGF-7. This could mean that interaction has an influence on both tissue remodeling and cancer growth.
Function
Studies have shown that FGF-7 expression is completely unregulated during minor or even chronic injury. This has lead researchers to believe that the protein is used to heal or repair epithelial cells. Furthermore, FGF-1 also triggers the formation of apical ectodermal ridge throughout the development of limbs in the body.
Recently, it has seemed to be the case that FGF-7 has been linked to skin injury repair, and has also been found to play some sort of role in breast cancer. As well as this, it is a vital regulator of HPC’s. It is vital because it can induce de novo activation of these HPCs.
Further research has shown that FGF6 is a niche signal that is required for the stimulation of adult liver progenitor cells and this can support liver regeneration. This research has lead to the suggestion that FGF7 could be a possibility therapeutic target for those suffering from liver diseases.
Studies like this are just one of the reasons why researchers continue to explore fgf-7, it’s functions and interactions.
Protein content
Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.9 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 KGF 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:

Precursor Brain-Derived Neurotrophic Factor Human Recombinant

proBDNF, Precursor Form Brain-derived Neurotrophic Factor.

Product # :

CYT-014

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Quantity :

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Description

proBDNF Human Recombinant produced in E.Coli is a single, non-glycosylated, non-covalently linked homodimer with each polypeptide chain containing 229 amino acids and having a molecular mass of 52kDa. The proBDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

proBDNF was lyophilized from a concentrated (0.5mg/ml) solution in 20mM PB, pH 8.0 and 500mM NaCl.

Purity

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

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Introduction
proBDNF (the precursor form of Brain-derived neurotrophic factor) interacts preferentially with p75NTR (the pan-neurotrophin receptor p75) and vps10p domain-containing receptor sortilin and induces neuronal apoptosis, while the mature BDNF selectively binds with great affinity to the TrkB kinase receptor and promotes the survival, growth and differentiation of neurons. Since proneurotrophins and mature neurotrophins bring forth opposite biological effects, proBDNF cleavage in the neuronal system is regulated in a specific and cell-context dependent manner. proBDNF has an important role in negative regulation of neurotrophic actions in the brain.
Synonyms
proBDNF, Precursor Form Brain-derived Neurotrophic Factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized proBDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution proBDNF 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 proBDNF in sterile 18M-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 Met-Ala-Pro-Met-Lys.
Background
Precursor Brain-Derived Neurotrophic Factor Human Recombinant: Unveiling the Potential of a Key Neurotrophic Factor
Abstract:
Precursor Brain-Derived Neurotrophic Factor (proBDNF) human recombinant is a pivotal neurotrophic factor that plays a critical role in neuronal development, survival, and synaptic plasticity. This research paper provides a comprehensive overview of proBDNF, including its characteristics, processing mechanisms, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of proBDNF human recombinant are proposed, highlighting its future implications in the field of neuroregenerative medicine.
Introduction:
Understanding the intricate processes underlying neuronal development and function is crucial for advancing neuroregenerative strategies. Neurotrophic factors, such as proBDNF, have garnered significant attention due to their pivotal roles in supporting neuronal growth and survival. This paper delves into the unique features of proBDNF and presents novel approaches for its production and optimization.
Characteristics and Processing Mechanisms:
proBDNF is a precursor protein consisting of 247 amino acids and is processed into mature brain-derived neurotrophic factor (mBDNF) through proteolytic cleavage. The ratio between proBDNF and mBDNF is tightly regulated and determines the balance between neuronal survival and apoptosis. Additionally, proBDNF exerts distinct biological functions through its receptor interactions, modulating synaptic plasticity and neuronal activity.
Production of proBDNF Human Recombinant:
Efficient production methodologies are essential to harness the therapeutic potential of proBDNF human recombinant. Various expression systems, including bacterial, yeast, and mammalian cell-based platforms, have been explored. Each system presents unique advantages and challenges, necessitating careful selection to achieve high yields and protein quality. Optimization strategies, such as codon optimization, fusion protein tags, and growth conditions, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to isolate high-quality proBDNF recombinant.
Potential Therapeutic Applications:
proBDNF human recombinant holds immense promise for neuroregenerative medicine. Its role in promoting neuronal survival, axonal growth, and synaptic plasticity positions it as a valuable therapeutic agent for neurodegenerative disorders, spinal cord injuries, and stroke. Additionally, the balance between proBDNF and mBDNF presents a potential therapeutic target for fine-tuning neuronal processes and restoring proper brain function.
Conclusion:
proBDNF human recombinant represents a crucial neurotrophic factor with diverse therapeutic applications in neuroregenerative medicine. Optimizing production methodologies and further understanding its processing mechanisms will enhance its clinical utility. With its potential implications in neurodegenerative disorders and neuronal repair, proBDNF human recombinant holds immense promise as a transformative tool for promoting neural health and regeneration.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 52kDa.

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

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

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

What is the amino acid sequence of BDNF Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Met-Lys.

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

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

Recombinant Human Mitogen-Activated Protein Kinase 1, His Tag

Mitogen-activated protein kinase 1, EC 2.7.11.24, Extracellular signal-regulated kinase 2, ERK-2, Mitogen-activated protein kinase 2, MAP kinase 2, MAPK 2, p42-MAPK, ERT1, ERK, p38, p40, p41, ERK2, MAPK2, PRKM1, PRKM2, P42MAPK, p41mapk.

Product # :

PKA-360

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Description

MAPK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 380 amino acids (1-360 a.a.) and having a molecular mass of 43.5 kDa. MAPK1 is fused to a 20 amino acids His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MAPK1 solution contains 20 mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Mitogen-activated protein kinase 1 (MAPK1) is also known as "extracellular signal-regulated kinase 2" (ERK2). Two similar (85% sequence identity) protein kinases were originally called ERK1 and ERK2. They were found during a search for protein kinases that are rapidly phosphorylated after activation of cell surface tyrosine kinases such as the epidermal growth factor receptor. Phosphorylation of ERKs leads to the activation of their kinase activity.The molecular events linking cell surface receptors to activation of ERKs are complex. It was found that Ras GTP-binding proteins are involved in the activation of ERKs. Another protein kinase, Raf-1, was shown to phosphorylate a "MAPK kinase", thus qualifying as a "MAPK kinase kinase". The MAPK kinase was named "MAPK/ERK kinase" (MEK). Receptor-linked tyrosine kinases, Ras, Raf, MEK and MAPK could be fitted into a signaling cascade linking an extracellular signal to MAPK activation Transgenic gene knockout mice lacking MAPK1 have major defe
Synonyms
Mitogen-activated protein kinase 1, EC 2.7.11.24, Extracellular signal-regulated kinase 2, ERK-2, Mitogen-activated protein kinase 2, MAP kinase 2, MAPK 2, p42-MAPK, ERT1, ERK, p38, p40, p41, ERK2, MAPK2, PRKM1, PRKM2, P42MAPK, p41mapk.
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 MAAAAAAGAG PEMVRGQVFD VGPRYTNLSY IGEGAYGMVC SAYDNVNKVR VAIKKISPFE HQTYCQRTLR EIKILLRFRH ENIIGINDII RAPTIEQMKD VYIVQDLMET DLYKLLKTQH LSNDHICYFL YQILRGLKYI HSANVLHRDL KPSNLLLNTT CDLKICDFGL ARVADPDHDH TGFLTEYVAT RWYRAPEIML NSKGYTKSID IWSVGCILAE MLSNRPIFPG KHYLDQLNHI LGILGSPSQE MGSSHHHHHH SSGLVPRGSH MAAAAAAGAG PEMVRGQVFD VGPRYTNLSY IGEGAYGMVC SAYDNVNKVR VAIKKISPFE HQTYCQRTLR EIKILLRFRH ENIIGINDII RAPTIEQMKD VYIVQDLMET DLYKLLKTQH LSNDHICYFL YQILRGLKYI HSANVLHRDL KPSNLLLNTT CDLKICDFGL ARVADPDHDH TGFLTEYVAT RWYRAPEIML NSKGYTKSID IWSVGCILAE MLSNRPIFPG KHYLDQLNHI LGILGSPSQE DLNCIINLKA RNYLLSLPHK NKVPWNRLFP NADSKALDLL DKMLTFNPHK RIEVEQALAH PYLEQYYDPS DEPIAEAPFK FDMELDDLPK EKLKELIFEE TARFQPGYRS.

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:

Glutathione S-Transferase MU 5 Human Recombinant, Active

Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.

Product # :

ENZ-997

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Description

GSTM5 Human Recombinant produced in E. coli is a single polypeptide chain containing 242 amino acids (1-218) and having a molecular mass of 28.2 kDa.GSTM5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GSTM5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 90,000 pmol/min/ug, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4- dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.

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Introduction
Glutathione S-transferase mu 5 (GSTM5) belongs to the glutathione s-transferase (GST) family of proteins. There are 8 families of GST proteins, specifically alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is comprised of proteins which have various functions throughout the cell. GSTM5 belongs to the mu class of enzymes which function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. GSTM5 has an imperative role in detoxification. GSTM5 conjugates reduced glutathione to a large number of exogenous and endogenous hydrophobic electrophiles.
Synonyms
Glutathione S-transferase mu 5, GSTM5-5, GST class-mu 5, GTM5, glutathione S-alkyltransferase M5, S-(hydroxyalkyl) glutathione lyase M5, EC 2.5.1.18.
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 MGSHMPMTLG YWDIRGLAHA IRLLLEYTDS SYVEKKYTLG DAPDYDRSQW LNEKFKLGLD FPNLPYLIDG AHKITQSNAI LRYIARKHNL CGETEEEKIR VDILENQVMD NHMELVRLCY DPDFEKLKPK YLEELPEKLK LYSEFLGKRP WFAGDKITFV DFLAYDVLDM KRIFEPKCLD AFLNLKDFIS RFEGLKKISA YMKSSQFLRG LLFGKSATWN SK.

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-23 Human Recombinant, His Tag

Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

Product # :

CYT-374

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Description

Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain expressed with a -6xHis tag containing a total of 257 amino acids (251 a.a. FGF23+ 6 a.a. His tag) and having a molecular mass of 28629.5 Dalton. The FGF-23 is and purified by chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (0.5mg/ml) was lyophilized from 25mM Tris pH7.5 and 0.6M NaCl solution.

Purity

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

Biological Activity

Treatment with hrFGF23 has been shown to induce FGFR mediated Erk phosphorylation, reduce plasma PTH levels in rats and to reduce blood phosphate levels.

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Introduction
FGF-23 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. FGF-23 inhibits renal tubular phosphate transport. This gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. Mutations FGF23 have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.
Synonyms
Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Lyophilized Fibroblast Growth Factor 23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 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 Fibroblast Growth Factor-23 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARN
SYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFR
GNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPG
MNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRAR
MTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRP
FAKFIHHHHHH.
Background
What is the molecular weight/Mw of FGF23 HUMAN, HIS Protein?
FGF23 HUMAN, HIS Protein has a total Mw of 28.6kDa.

What is the source or expression system of FGF23 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of FGF23 HUMAN, HIS Protein?
FGF23 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF23 HUMAN, HIS Protein?
Treatment with hrFGF23 has been shown to induce FGFR mediated Erk phosphorylation, reduce plasma PTH levels in rats and to reduce blood phosphate levels.

What is the amino acid sequence of FGF23 HUMAN, HIS Protein?
MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARN
SYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFR
GNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPG
MNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRAR
MTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRP
FAKFIHHHHHH.

What applications can FGF23 HUMAN, HIS Protein be used in?
FGF23 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF23 HUMAN, HIS Protein?
The endotoxin level is minimal, FGF23 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:

Nanog Human Recombinant, His Tag

NANOG, Homeobox protein NANOG, Homeobox transcription factor Nanog, hNanog.

Product # :

PRO-881

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Description

NANOG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154) and having a molecular mass of 19.6 kDa.The NANOG is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NANOG protein (0.25mg/ml) is supplied in 20mM Tris-HCL, pH-8, 1mM DTT and 20% Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
NANOG is a multidomain homeobox transcription factor which functions to maintain the undifferentiated state of pluripotent stem cells. NANOG expression counteracts the differentiation-promoting signals induced by the extrinsic factors LIF, Stat3 and BMP. Once NANOG expression is downregulated, cell differentiation can proceed. Proteins which regulate NANOG expression include transcription factors Oct4, SOX2, FoxD3, and Tcf3 and tumor suppressor p53.
Synonyms
NANOG, Homeobox protein NANOG, Homeobox transcription factor Nanog, hNanog.
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 MSVDPACPQS LPCFEASDCK ESSPMPVICG PEENYPSLQM SSAEMPHTET VSPLPSSMDL LIQDSPDSST SPKGKQPTSA EKSVAKKEDK VPVKKQKTRT VFSSTQLCVL NDRFQRQKYL SLQQMQELSN ILNLSYKQVK TWFQNQRMKS KRWQ

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 1 Rat Recombinant

GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.

Product # :

CYT-1012

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Description

GFRA1 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 645 amino acids (25-430a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA1 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GFRA1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.
Synonyms
GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.
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
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK 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 GFRA1 RAT Protein?
GFRA1 RAT Protein has a total Mw of 72.3kDa.

What is the source or expression system of GFRA1 RAT Protein?
Sf9, Baculovirus cells.

What is the Purity of GFRA1 RAT Protein?
GFRA1 RAT Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of GFRA1 RAT Protein?
The biological functionality of GFRA1 RAT Protein will be determined in the future.

What is the amino acid sequence of GFRA1 RAT Protein?
DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK 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 GFRA1 RAT Protein be used in?
GFRA1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GFRA1 RAT Protein?
The endotoxin level is minimal, GFRA1 RAT 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:

Fibroblast Growth Factor Receptor-2 Human Recombinant, His Tag

EC 2.7.10, FGFR-2, BFR-1, CD332, BBDS, CEK3, ECT1, TK14, TK25, CFD1, KSAM, JWS, Fibroblast Growth Factor Receptor 2, Keratinocyte Growth Factor Receptor, Bacteria-Expressed Kinase, EC 2.7.10.1, K-SAM, KGFR, BEK, Protein Tyrosine Kinase, Receptor Like 14, BEK Fibroblast Growth Factor Receptor, Craniofacial Dysostosis 1, Jackson-Weiss Syndrome, Pfeiffer Syndrome, Crouzon Syndrome, CD332 Antigen.

Product # :

PKA-098

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Description

FGFR2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 596 amino acids (22-378a.a.) and having a molecular mass of 66.6kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).FGFR2 is expressed with a 239 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FGFR2 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Fibroblast Growth Factors (FGFs) comprise a family of at least eighteen structurally realted proteins that are involved in a multitude of physiological and pathological cellular processes, including cell growth, differentation, angiogenesis, wound healing and tumorgenesis. The biological activities of the FGFs are mediated by a family if type I transmembrane tyrosine kinases which undergo dimerization and autophosphorylation after ligand binding. Four distinct genes encoding closely related FGF receptors, FGFR-1to -4 are known. Multiple forms of FGFR-1 to -3 are generated by alternative splicing of the mRNAs. A frequent splicing event involving FGFR-1 and -2 results in receptors containing all three Ig domains, referred to as the alpha isoform, or only IgII and IgIII, referred to as the ? isoform. Only the alpha isoform has been identified for FGFR-3 and FGFR-4. Additional splicing events for FGFR-1 to -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 FGFR-1. Mutations in FGFR-1 to -3 have been found in patients with birth defects involving craniosynostosis.
Synonyms
EC 2.7.10, FGFR-2, BFR-1, CD332, BBDS, CEK3, ECT1, TK14, TK25, CFD1, KSAM, JWS, Fibroblast Growth Factor Receptor 2, Keratinocyte Growth Factor Receptor, Bacteria-Expressed Kinase, EC 2.7.10.1, K-SAM, KGFR, BEK, Protein Tyrosine Kinase, Receptor Like 14, BEK Fibroblast Growth Factor Receptor, Craniofacial Dysostosis 1, Jackson-Weiss Syndrome, Pfeiffer Syndrome, Crouzon Syndrome, CD332 Antigen.
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
RPSFSLVEDT TLEPEEPPTK YQISQPEVYV AAPGESLEVR CLLKDAAVIS WTKDGVHLGP NNRTVLIGEY LQIKGATPRD SGLYACTASR TVDSETWYFM VNVTDAISSG DDEDDTDGAE DFVSENSNNK RAPYWTNTEK MEKRLHAVPA ANTVKFRCPA GGNPMPTMRW LKNGKEFKQE HRIGGYKVRN QHWSLIMESV VPSDKGNYTC VVENEYGSIN HTYHLDVVER SPHRPILQAG LPANASTVVG GDVEFVCKVY SDAQPHIQWI KHVEKNGSKY GPDGLPYLKV LKHSGINSSN AEVLALFNVT EADAGEYICK VSNYIGQANQ SAWLTVLPKQ QAPGREKEIT ASPDYLELEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK 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:

Mitogen-Activated Protein Kinase 10 Human Recombinant

C-Jun N-Terminal Kinase 3, MAP Kinase P49 3F12, MAP Kinase 10, PRKM10, SAPK1b, JNK3A, JNK3.

Product # :

PKA-115

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Description

MAPK10 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 470 amino acids (1-464 a.a.) and having a molecular mass of 53.4kDa. MAPK10 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

MAPK10 is protein solution ( 0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4), 30% glycerol, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
MAPK10 is part of the MAP kinase protein family. MAP Kinases perform as assimilation point for many biochemical pathways. The enzyme also takes part in wide range of cellular pathways: differentiation, proliferation, development and transcription regulation.
Synonyms
C-Jun N-Terminal Kinase 3, MAP Kinase P49 3F12, MAP Kinase 10, PRKM10, SAPK1b, JNK3A, JNK3.
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
MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS VEVGDSTFTV LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ NQTHAKRAYR ELVLMKCVNH KNIISLLNVF TPQKTLEEFQ DVYLVMELMD ANLCQVIQME LDHERMSYLL YQMLCGIKHL HSAGIIHRDL KPSNIVVKSD CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY KENVDIWSVG CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV DDALQHPYIN VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN SEEKTKNGVV KGQPSPSGAA VNSSESLPPS SSVNDISSMS TDQTLASDTD SSLEASAGPL GCCRHHHHHH.

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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