Search: 1000 results found for "Beta-NGF"

Description:

Nuclear Receptor Binding Factor 2 Human Recombinant

Nuclear receptor binding factor 2, COPR1, COPR2, NRBF-2, Nuclear receptor-binding factor 2, Comodulator of PPAR and RXR, NRBF2, COPR.

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PRO-1692

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Description

NRBF2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (45-287) and having a molecular mass of 29.9 kDa.NRBF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NRBF2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Nuclear receptor binding factor 2 (NRBF2) which works as transcriptional activator, modulates transcriptional activation by target nuclear receptors.
Synonyms
Nuclear receptor binding factor 2, COPR1, COPR2, NRBF-2, Nuclear receptor-binding factor 2, Comodulator of PPAR and RXR, NRBF2, COPR.
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 MGSMKLTQSE QAHLSLELQR DSHMKQLLLI QERWKRAQRE ERLKAQQNTD KDAAAHLQTS HKPSAEDAEG QSPLSQKYSP STEKCLPEIQ GIFDRDPDTL LYLLQQKSEP AEPCIGSKAP KDDKTIIEEQ ATKIADLKRH VEFLVAENER LRKENKQLKA EKARLLKGPI EKELDVDADF VETSELWSLP PHAETATASS TWQKFAANTG KAKDIPIPNL PPLDFPSPEL PLMELSEDIL KGFMNN.

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-13 Human Recombinant

Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

Product # :

CYT-938

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Description

BMP13 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.1kDa.The BMP-13 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP-13 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

Purity

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

Biological Activity

The ED₅₀ as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

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Introduction
Growth/differentiation factors (GDF1-GDF15) belong to the BMP family of TGF-beta superfamily proteins. These factors are produced as inactive preproproteins which are subsequently cleaved and assembled into active secreted homodimers. BMP13 is a growth factor which controls proliferation and cellular differentiation in the retina and bone formation. BMP13 has a central role in regulating apoptosis during retinal development. GDF proteins are vital during embryonic development, particularly in the skeletal, nervous, and muscular systems. BMP13 gene mutations result in colobomata, which are congenital abnormalities in ocular development, and in Klippel-Feil syndrome (KFS), which is a congenital disorder of spinal segmentation.
Synonyms
Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BMP13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-13 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 BMP13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.
Background
Bone Morphogenetic Protein-13 Human Recombinant: Unraveling its Potential in Tissue Engineering and Regenerative Medicine
Abstract:
Bone Morphogenetic Protein-13 (BMP-13) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-13, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-13 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.
Introduction:
Tissue engineering and regenerative medicine hold great promise in addressing tissue repair and regeneration challenges. BMP-13, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the distinctive features of BMP-13 and presents novel approaches for the production and optimization of BMP-13 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-13 is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intricate intracellular signaling cascades. BMP-13 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate critical processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.
Production of BMP-13 Human Recombinant:
Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-13 human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-13. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-13 recombinant protein.
Potential Therapeutic Applications:
BMP-13 human recombinant holds immense promise in the field of tissue engineering and regenerative medicine. Its involvement in cartilage formation, osteogenesis, and tissue repair makes it a potential candidate for the treatment of musculoskeletal disorders, joint injuries, and cartilage defects. Furthermore, the ability of BMP-13 to modulate cell behavior and tissue remodeling indicates its wider therapeutic applications in diverse regenerative processes.
Conclusion:
BMP-13 human recombinant emerges as a crucial regulator in tissue engineering and regenerative medicine, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will undoubtedly enhance its therapeutic applications. Given its involvement in cartilage and bone formation, as well as tissue repair, BMP-13 human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.
What is the molecular weight/Mw of GDF6 Protein?
GDF6 Protein has a total Mw of 27.1kDa.

What is the source or expression system of GDF6 Protein?
Escherichia Coli.

What is the Purity of GDF6 Protein?
GDF6 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF6 Protein?
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

What is the amino acid sequence of GDF6 Protein?
TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

What applications can GDF6 Protein be used in?
GDF6 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF6 Protein?
The endotoxin level is minimal, GDF6 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:

Ubiquitin-Conjugating Enzyme E2F Human Recombinant

Ubiquitin-conjugating enzyme E2F (putative), NEDD8 carrier protein UBE2F, NEDD8 protein ligase UBE2F, NEDD8-conjugating enzyme 2, NEDD8-conjugating enzyme UBE2F, NCE2, EC 6.3.2.-.

Product # :

ENZ-625

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Description

UBE2F Human Recombinant produced in E. coli is a single polypeptide chain containing 209 amino acids (1-185) and having a molecular mass of 23.7 kDa.UBE2F is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The UBE2F solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 1mM DTT and 30% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Ubiquitin-conjugating enzyme E2 F (UBE2F) is a member of the ubiquitin-conjugating enzyme family and UBE2F subfamily. Ubiquitin-conjugating enzymes or sometimes as ubiquitin-carrier enzymes, run the second step in the ubiquitination reaction which targets a protein for degradation using the proteasome. The UBE2F receives the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins.
RBX2-UBE2F complex neddylates specific target proteins, for example CUL5 as can be seen from the specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1.
Synonyms
Ubiquitin-conjugating enzyme E2F (putative), NEDD8 carrier protein UBE2F, NEDD8 protein ligase UBE2F, NEDD8-conjugating enzyme 2, NEDD8-conjugating enzyme UBE2F, NCE2, EC 6.3.2.-.
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 MGSHMLTLAS KLKRDDGLKG SRTAATASDS TRRVSVRDKL LVKEVAELEA NLPCTCKVHF PDPNKLHCFQ LTVTPDEGYY QGGKFQFETE VPDAYNMVPP KVKCLTKIWH PNITETGEIC LSLLREHSID GTGWAPTRTL KDVVWGLNSL FTDLLNFDDP LNIEAAEHHL RDKEDFRNKV DDYIKRYAR

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:

Ring Finger Protein 34 Human Recombinant

Ring Finger Protein 34, E3 Ubiquitin Protein Ligase, RING Finger Protein 34, Caspase Regulator CARP1, Caspases-8 And -10-Associated RING Finger Protein 1, FYVE-RING Finger Protein Momo, Human RING Finger Homologous To Inhibitor Of Apoptosis Protein, CARP-1, hRFI, RING Finger Protein RIFF, RFI, CARP1, RIF, RIFF, E3 Ubiquitin-Protein Ligase RNF34, EC 6.3.2.

Product # :

PRO-1761

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Description

RNF34 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373a.a) and having a molecular mass of 44.2kDa.RNF34 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RNF34 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Ring Finger Protein 34 (RNF34) has E3 ubiquitin-protein ligase activity. RNF34 has a RINF finger, a motif recognized to be involved in protein-protein and protein-DNA interactions. RNF34 regulates the levels of CASP8 and CASP10 by targeting them for proteasomal degradation. In addition, RNF34 protects cells against apoptosis induced by TNF. RNF34 also binds phosphatidylinositol 5-phosphateand phosphatidylinositol 3-phosphate. Alternatively splicing results in multiple transcript variants encoding distinct isoforms.
Synonyms
Ring Finger Protein 34, E3 Ubiquitin Protein Ligase, RING Finger Protein 34, Caspase Regulator CARP1, Caspases-8 And -10-Associated RING Finger Protein 1, FYVE-RING Finger Protein Momo, Human RING Finger Homologous To Inhibitor Of Apoptosis Protein, CARP-1, hRFI, RING Finger Protein RIFF, RFI, CARP1, RIF, RIFF, E3 Ubiquitin-Protein Ligase RNF34, EC 6.3.2.
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 MGS MRKAGAT SMWASCCGLL NEVMGTGAVR GQQSAFAGAT GPFRFTPNPE FSTYPPAATE GPNIVCKACG LSFSVFRKKH VCCDCKKDFC SVCSVLQENL RRCSTCHLLQ ETAFQRPQLM RLKVKDLRQY LILRNIPIDT CREKEDLVDL VLCHHGLGSE DDMDTSSLNS SRSQTSSFFT RSFFSNYTAP SATMSSFQGE LMDGDQTSRS GVPAQVQSEI TSANTEDDDD DDDEDDDDEE ENAEDRNPGL SKERVRASLS DLSSLDDVEG MSVRQLKEIL ARNFVNYSGC CEKWELVEKV NRLYKENEEN QKSYGERLQL QDEEDDSLCR ICMDAVIDCV LLECGHMVTC TKCGKRMSEC PICRQYVVRA VHVFKS

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:

Epidermal Growth Factor Receptor Human Recombinant Sf9, Active

Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.

Product # :

PKA-335

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Description

EGFR Human Recombinant encoding a.a. 672-1210 expressed in Baculovirus infected Sf9 cells, fused with a GST-tag at N-terminus with thrombin cleavage sites, having a molecular weight of 89,171 Dalton.EGFR is purified by proprietary chromatographic techniques.

Source

Baculovirus infected Sf9 cells.

Formulation

EGFR in 50mM HEPES pH 7.5, 100mM NaCl, 5mM DTT, 15mM reduced glutathione and 20% glycerol.

Biological Activity

Determination of Km value by Filter binding assay MAFC membrane.

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Introduction
The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-a , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.
Synonyms
Epidermal growth factor receptor, EC 2.7.10.1, Receptor tyrosine-protein kinase ErbB-1, ERBB, mENA, ERBB1, EGFR.
Physical Appearance
Sterile filtered liquid.
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Please avoid freeze-thaw cycles.
Specific Activity
30 pmol/µgxmin.

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:

GRO-Beta Human Recombinant (CXCL2)

Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

Product # :

CHM-309

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Description

GRO-Beta Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7908 Dalton. The CXCL2 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 Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

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Introduction
Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.
Synonyms
Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CXCL2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 GRO-beta Human 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-Pro-Leu-Ala-Thr.
Background
What is the molecular weight/Mw of CXCL2 HUMAN Protein?
CXCL2 HUMAN Protein has a total Mw of 7.9kDa.

What is the source or expression system of CXCL2 HUMAN Protein?
Escherichia Coli.

What is the Purity of CXCL2 HUMAN Protein?
CXCL2 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL2 HUMAN Protein?
The Biological activity is calculated by its ability to chemoattract CXCR2 transfected 293 cells using 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CXCL2 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Leu-Ala-Thr.

What applications can CXCL2 HUMAN Protein be used in?
CXCL2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL2 HUMAN Protein?
The endotoxin level is minimal, CXCL2 HUMAN 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-21 Mouse Recombinant, Sf9

Fibroblast growth factor 21, FGF-21.

Product # :

CYT-930

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Description

FGF-21 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (29-210a.a.) and having a molecular mass of 21.0kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). FGF21 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FGF-21 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in ? cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents.
Synonyms
Fibroblast growth factor 21, FGF-21.
Physical Appearance
Sterile Filtered colorless 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
AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALK PGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDAT SWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY ASLEHHHHHH.
Background
What is the molecular weight/Mw of FGF21 MOUSE,SF9 Protein?
FGF21 MOUSE,SF9 Protein has a total Mw of 21kDa.

What is the source or expression system of FGF21 MOUSE,SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of FGF21 MOUSE,SF9 Protein?
FGF21 MOUSE,SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF21 MOUSE,SF9 Protein?
The biological functionality of FGF21 MOUSE,SF9 Protein will be determined in the future.

What is the amino acid sequence of FGF21 MOUSE,SF9 Protein?
AYPIPDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGAAHRSP ESLLELKALK PGVIQILGVK ASRFLCQQPD GALYGSPHFD PEACSFRELL LEDGYNVYQS EAHGLPLRLP QKDSPNQDAT SWGPVRFLPM PGLLHEPQDQ AGFLPPEPPD VGSSDPLSMV EPLQGRSPSY ASLEHHHHHH.

What applications can FGF21 MOUSE,SF9 Protein be used in?
FGF21 MOUSE,SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF21 MOUSE,SF9 Protein?
The endotoxin level is minimal, FGF21 MOUSE,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:

Beta Defensin 118 Human Recombinant

Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

Product # :

CYT-714

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Description

DEFB118 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (21-123 a.a) and having a molecular mass of 13.8kDa.DEFB118 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DEFB118 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Beta Defensin 118 (DEFB118) which is a member of the beta subfamily of defensins, is found in a cluster with other beta-defensin genes on the long arm of chromosome 20. Beta-defensins are antimicrobial peptides which provide protection for tissues and organs from infection by a diversity of microorganisms. DEFB118 protein’s expression is regulated by androgen, and the encoded protein binds to sperm and exhibits antibacterial activity.
Synonyms
Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.
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 MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.
Background
Title: Beta Defensin 118 Human Recombinant: Exploring its Role in Innate Immunity and Potential Therapeutic Applications
Abstract:

Beta defensin 118 (BD118) is a member of the beta defensin family, known for its antimicrobial properties and immune-modulatory functions. This research paper provides a comprehensive analysis of human recombinant BD118, focusing on its production, characterization, and potential applications in immune modulation and therapeutic interventions. The paper highlights the significance of BD118 in innate immunity and its role in host defense against microbial pathogens. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD118 in various inflammatory and infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD118 and its utility as a research tool and a potential immunotherapeutic agent.
Introduction:

Beta defensin 118 (BD118) is a small cationic peptide that plays a critical role in the innate immune response against microbial pathogens. Human recombinant BD118, generated through genetic engineering techniques, offers a valuable tool for studying its immune-modulatory properties and exploring its therapeutic potential.
Production and Characterization:

Recombinant BD118 is typically produced using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD118.
Role in Innate Immunity:

BD118 exhibits antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Additionally, it possesses immune-modulatory functions, such as the regulation of pro-inflammatory responses and the promotion of wound healing. Recombinant BD118 serves as a valuable tool for investigating the mechanisms underlying its immune-modulatory actions and exploring its potential as an immunotherapeutic agent.
Therapeutic Implications:

Dysregulation of the immune system is associated with various inflammatory and infectious diseases. Recombinant BD118 holds promise as a potential therapeutic agent due to its antimicrobial properties and immune-modulatory functions. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD118 in conditions such as skin infections, respiratory diseases, and inflammatory bowel disease.
Conclusion:

Human recombinant BD118 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune modulation contribute to our understanding of innate immunity and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD118 offer promising avenues for improving outcomes in inflammatory and infectious diseases.
What is the molecular weight/Mw of DEFB118 Protein?
DEFB118 Protein has a total Mw of 13.8kDa.

What is the source or expression system of DEFB118 Protein?
Escherichia Coli.

What is the Purity of DEFB118 Protein?
DEFB118 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of DEFB118 Protein?
The biological functionality of DEFB118 Protein will be determined in the future.

What is the amino acid sequence of DEFB118 Protein?
MGSSHHHHHH SSGLVPRGSH MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

What applications can DEFB118 Protein be used in?
DEFB118 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for DEFB118 Protein?
The endotoxin level is minimal, DEFB118 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:

Crystallin Beta B1 Human Recombinant

EC 1.17.4.1, RR2M, Beta-B1 crystallin, CATCN3.

Product # :

HSP-033

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Description

CRYBB1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (1-252 a.a.) and having a molecular mass of 29.1 kDa. The CRYBB1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CRYBB1 solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Crystallins are the main structural proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into 3 fprotein families, α, β, & γ families. Because lens central fiber cells lose their nuclei during development, these crystallins are prepared and then retained throughout life, making them extremely stable proteins. CRYBB1 is a beta basic group member and undergoes extensive cleavage at its N-terminal extension during lens maturation.
Synonyms
EC 1.17.4.1, RR2M, Beta-B1 crystallin, CATCN3.
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
MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE GSFPVLATEP PKRSHHHHHH.

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:

Core 1 Beta3-Gal-T1 Human Recombinant

Core 1 Synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Core 1 Beta3-Gal-T1, Core 1 O-Glycan T-Synthase, Core 1 UDP-Galactose:N-Acetylgalactosamine-Alpha-R Beta 1,3 Galactosyltransferase 1, B3Gal-T8, EC 2.4.1.122, Core 1 Beta3-Gal-T, C1GALT, T-synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Beta-1,3-galactosyltransferase, C1GalT1, Core 1 Beta1,3-Galactosyltransferase 1.

Product # :

ENZ-721

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Description

C1GALT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (30-363 a.a) and having a molecular mass of 41.4kDa.C1GALT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

C1GALT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Core 1 Beta3-Gal-T1 also known as,C1GALT1 creates the common core 1 O-glycan structure, Gal-beta-1-3GalNAc-R, by the transfer of Gal from UDP-Gal to GalNAc-alpha-1-R. Core 1 is a precursor for lots of extended mucin-type O-glycans on cell surface and secreted glycoproteins. Studies in mice have shown that this gene takes a main role in angiogenesis, thrombopoiesis and kidney homeostasis.
Synonyms
Core 1 Synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Core 1 Beta3-Gal-T1, Core 1 O-Glycan T-Synthase, Core 1 UDP-Galactose:N-Acetylgalactosamine-Alpha-R Beta 1,3 Galactosyltransferase 1, B3Gal-T8, EC 2.4.1.122, Core 1 Beta3-Gal-T, C1GALT, T-synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Beta-1,3-galactosyltransferase, C1GalT1, Core 1 Beta1,3-Galactosyltransferase 1.
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 MGSLLGEKVD TQPNVLHNDP HARHSDDNGQ NHLEGQMNFN ADSSQHKDEN TDIAENLYQK VRILCWVMTG PQNLEKKAKH VKATWAQRCN KVLFMSSEEN KDFPAVGLKT KEGRDQLYWK TIKAFQYVHE HYLEDADWFL KADDDTYVIL DNLRWLLSKY DPEEPIYFGR RFKPYVKQGY MSGGAGYVLS KEALKRFVDA FKTDKCTHSS SIEDLALGRC MEIMNVEAGD SRDTIGKETF HPFVPEHHLI KGYLPRTFWY WNYNYYPPVE GPGCCSDLAV SFHYVDSTTM YELEYLVYHL RPYGYLYRYQ PTLPERILKE ISQANKNEDT KVKLGNP.

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:

GM-CSF Receptor Alpha Human Recombinant

CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.

Product # :

CYT-796

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sds-page

Description

CSF2RA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (20-320 a.a) and having a molecular mass of 37.2kDa.CSF2RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CSF2RA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

sds-page

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Introduction
GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.
Synonyms
CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor 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. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Background
Unlocking the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Implications and Applications
Abstract:
The Ciliary Neurotrophic Factor Receptor (CNTFR) plays a pivotal role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper examines the significance of Human Recombinant CNTFR, its production techniques, and its potential applications in neurobiology and therapeutic interventions. The review underscores CNTFR's crucial role in advancing neuroprotection and neuroregeneration research.
Introduction:
CNTFR, a transmembrane protein, is central to transducing the signals initiated by CNTF. Availability of Human Recombinant CNTFR enables researchers to dissect its contribution to neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's role in modulating neuronal health and promoting regeneration makes it a cornerstone in neurobiology.
Role in CNTF Signaling:
CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and trigger downstream signaling pathways. Activation of intracellular cascades, such as JAK/STAT and MAPK, is instrumental in driving the neuroprotective and growth-promoting effects of CNTF.
Production Methods:
Human Recombinant CNTFR is generated through gene expression in suitable host cells, often utilizing bacterial or mammalian systems. Ensuring accurate folding and post-translational modifications is crucial to preserve its functionality and affinity for CNTF.
Therapeutic Applications:
Human Recombinant CNTFR holds promise for therapeutic applications in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-associated signaling presents opportunities to bolster neuronal survival and regeneration, potentially revolutionizing patient care.
Challenges and Future Directions:
While the potential is significant, challenges encompass optimizing CNTFR-CNTF interactions, effective tissue delivery, and understanding potential off-target effects. Ongoing research is paramount to unravel the complete mechanisms of CNTFR-mediated signaling and its therapeutic implications.
Conclusion:
Human Recombinant Ciliary Neurotrophic Factor Receptor emerges as a vital tool in advancing our grasp of neuroprotection and regeneration. Its capacity to modulate CNTF effects opens doors to innovative therapeutic strategies for addressing neurodegenerative disorders, embodying the intersection of molecular insights and clinical progress.
What is the molecular weight/Mw of CD116 Protein?
CD116 Protein has a total Mw of 37.2kDa.

What is the source or expression system of CD116 Protein?
Escherichia Coli.

What is the Purity of CD116 Protein?
CD116 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of CD116 Protein?
The biological functionality of CD116 Protein will be determined in the future.

What is the amino acid sequence of CD116 Protein?
CD116 Protein is composed from 324 amino acids.

What applications can CD116 Protein be used in?
CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD116 Protein?
The endotoxin level is minimal, CD116 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:

NTF2-like Export Factor 2 Human Recombinant

NTF2-related export protein 2, Protein p15-2, NXT2, BM-025, DC9, P15-2.

Product # :

PRO-1051

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Description

NXT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-197 a.a) and having a molecular mass of 25.3kDa.NXT2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

NXT2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 40% glycerol and 200mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Nuclear transport factor 2-like export factor 2 (NXT2) belongs to the NXT family proteins which are commonly involved in exporting nuclear RNA in eukaryotic cells. The NXT2 protein is a regulator of protein export for NES-containing proteins. In addition, NXT2 associates with NXF1, NXF2, NXF3 and NXF5 and has a role in mRNA nuclear export. NXT2 has a critical role in upholding morphogenetic integrity of embryonic heart in vertebrate species. The NXT2 protein contains a nuclear transport factor 2 (NTF2) domain, which has a vital role in the trafficking of macromolecules, ions, and small molecules between the cytoplasm and nucleus, it may also have a role in mRNA nuclear export.
Synonyms
NTF2-related export protein 2, Protein p15-2, NXT2, BM-025, DC9, P15-2.
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 MGSHMRKYRS HWSQGDREGY QRRSNYYEGP HTSHSSPADR TREEVVTPTL PEHTATRSQM ATSLDFKTYV DQACRAAEEF VNIYYETMDK RRRALTRLYL DKATLIWNGN AVSGLDALNN FFDTLPSSEF QVNMLDCQPV HEQATQSQTT VLVVTSGTVK
FDGNKQHFFN QNFLLTAQST PNNTVWKIAS DCFRFQDWSS 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:

Transforming Growth Factor-Beta 3 Human Recombinant, CHO

Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

Product # :

CYT-1259

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Description

TGFB3 Human Recombinant produced in CHO cells is a glycosylated, polypeptide homodimer chain containing 2x112 amino acids and having a total molecular mass of 25.0kDa. The TGFB3 is purified by proprietary chromatographic techniques.

Source

CHO cells.

Formulation

TGFB3 was lyophilized from a concentrated solution containing 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.

Purity

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

Biological Activity

The ED₅₀ as determined by its ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0 × 10⁷ units/mg.

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Synonyms
Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Transforming Growth Factor-Beta 3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 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 TGFB3 in sterile 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.
Background
Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. 3 TGF Betas have been identified in mammals: TGF Beta 1, TGF Beta 2 and TGF Beta 3. each are synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

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:

Beta Defensin-3 Rat Recombinant

Beta-defensin 3, BD-3, Defensin beta 3, Defb3.

Product # :

CYT-063

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Description

BD-3 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.5kDa.The BD-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BD-3 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

Measured by its antimicrobial activity against E. coli. The ED₅₀ for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

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Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
Synonyms
Beta-defensin 3, BD-3, Defensin beta 3, Defb3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BD-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized BD-3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
KKVYNAVSCM TNGGICWLKC SGTFREIGSC GTRQLKCCKK K.
Background
What is the molecular weight/Mw of BD3 Protein?
BD3 Protein has a total Mw of 4.5kDa.

What is the source or expression system of BD3 Protein?
Escherichia Coli.

What is the Purity of BD3 Protein?
BD3 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of BD3 Protein?
Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 4-20µg/ml, corresponding to a specific activity of 50,000-250,000units/mg.

What is the amino acid sequence of BD3 Protein?
KKVYNAVSCM TNGGICWLKC SGTFREIGSC GTRQLKCCKK K.

What applications can BD3 Protein be used in?
BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD3 Protein?
The endotoxin level is minimal, BD3 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:

Epidermal Growth Factor Mouse Recombinant, His Tag

Urogastrone, URG, EGF.

Product # :

CYT-138

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SDS-PAGE

Description

EGF mouse Recombinant produced in E. coli is a single polypeptide chain containing 77 amino acids (977-1029) and having a molecular mass of 8.6kDa.EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The EGF solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
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 MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
Background
Unveiling Epidermal Growth Factor Mouse Recombinant: Harnessing His Tag for Enhanced Insights and Therapeutic Prospects
Abstract:
This research paper delves into the realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), focusing on the strategic integration of a Histidine (His) Tag. By employing sophisticated methodologies encompassing protein engineering, chromatographic techniques, and cellular assays, this study unveils the multifaceted molecular attributes of EGF-MR with His Tag. The findings not only enhance our understanding of EGF-MR's behavior but also illuminate potential avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) governs vital cellular processes. This paper delves into Epidermal Growth Factor Mouse Recombinant (EGF-MR) with a specific emphasis on the incorporation of a Histidine (His) Tag, unraveling its molecular intricacies and therapeutic implications.
Protein Engineering and His Tag Integration:
The paper navigates the tailored engineering of EGF-MR to accommodate a His Tag, a peptide sequence that facilitates protein purification. The process involves strategic modification of the EGF-MR gene to ensure proper folding and presentation of the His Tag.
Chromatographic Purification and His Tag Affinity:
Chromatographic techniques, specifically immobilized metal ion affinity chromatography (IMAC), are employed to purify the His-tagged EGF-MR. The His Tag's high affinity for metal ions facilitates efficient purification, yielding a highly purified and bioactive protein product.
Structural and Functional Insights:
The presence of the His Tag is not just for purification; it serves as a molecular handle to investigate EGF-MR's structural dynamics. High-resolution structural analyses coupled with biophysical assays unravel how the His Tag affects EGF-MR's conformation and binding interactions.
Cellular Assays and Bioactivity Assessment:
In vitro cellular assays, including proliferation and migration studies, provide insights into the impact of His Tag on EGF-MR's bioactivity. Comparative analyses shed light on the functionality of His-tagged EGF-MR and its potential implications in cellular responses.
Therapeutic Prospects and Targeted Delivery:
The incorporation of a His Tag presents a unique avenue for tailored drug delivery. The His Tag can serve as a docking site for targeted therapies, enabling precise interactions with specific receptors on target cells.
Future Directions and Challenges:
While promising, challenges such as potential steric hindrance from the His Tag require consideration. Future research should focus on optimizing the positioning of the His Tag to maintain EGF-MR's full biological activity.
Conclusion:
In a harmonious synthesis of advanced methodologies and innovative insights, the integration of His Tag into Epidermal Growth Factor Mouse Recombinant emerges as a transformative paradigm. The His Tag not only facilitates purification but also offers a molecular window into EGF-MR's behavior, potentially redefining targeted therapies and precision medicine.
What is the molecular weight/Mw of EGF MOUSE, HIS Protein?
EGF MOUSE, HIS Protein has a total Mw of 8.6kDa.

What is the source or expression system of EGF MOUSE, HIS Protein?
Escherichia Coli.

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

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

What is the amino acid sequence of EGF MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.

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

What is the endotoxin level for EGF MOUSE, HIS Protein?
The endotoxin level is minimal, EGF MOUSE, 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:

Human Vascular Endothelial Growth Inhibitor Recombinant

Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.

Product # :

CYT-517

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Quantity :

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Shipped at Room temp

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Description

TNFSF15 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 20.5kDa. The TNFSF15 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TNFSF15 was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 with 0.02% Tween-20.

Purity

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

Biological Activity

The ED50 as determined by its ability to induce apoptosis using human TF-1 cells is less than 20ng/ml, corresponding to a specific activity of > 5.0×10⁴ IU/mg.

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Introduction
TNFSF15 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is abundantly expressed in endothelial cells, but is not expressed in either B or T cells. The expression of TNFSF15 is inducible by TNF and IL-1 alpha. This cytokine is a ligand for receptor TNFRSF25 and decoy receptor TNFRSF21/DR6. It can activate NF-kappaB and MAP kinases, and acts as an autocrine factor to induce apoptosis in endothelial cells. TNFSF15 is also found to inhibit endothelial cell proliferation, and thus may function as an angiogenesis inhibitor. An additional isoform encoded by an alternatively spliced transcript variant has been reported but the sequence of this transcript has not been determined.
Synonyms
Tumor necrosis factor ligand superfamily member 15, TNFSF-15, TNFSF15, TNF ligand-related molecule 1, VEGI, TL-1, TL1, TL1A, VEGI192A, VEGI-192, MGC129934, MGC129935.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
TNFSF15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGI 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 TNFSF15 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MQLTKGRLHFSHPLSHTKHISPFVTDAPLRADGDKPRAHL
TVVRQTPTQHFKNQFPALHWEHELGLAFTKNRMNYTNKF
LLIPESGDYFIYSQVTFRGMTSECSEIRQAGRPNKPDSIT
VVITKVTDSYPEPTQLLMGTKSVCEVGSNWFQPIYLGAM
FSLQEGDKLMVNVSDISLVDYTKEDKTFFGAFLL.

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:

Beta-Synuclein Human Recombinant

Beta-synuclein, SNCB, b-Synuclein.

Product # :

PRO-394

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Description

Recombinant Human b-Synuclein produced in E.Coli is a single, non-glycosylated polypeptide chain (1-134 a.a) having a molecular mass of 14.2kDa (molecular size on SDS-PAGE will appear higher).

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.1M NaCl and 1mM MgCl2.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
b-synuclein (amino acids 1-134), an acidic neuronal protein of 134 amino acids, is extremely heat-resistant. b-synucelin also has a chaperone-like activity. Recently, b-synuclein has been suggested to inhibit a-synuclein aggregation. b and a-synuclein are abundantly expressed in the brain and putatively inhibit phospholipase D2 selectively. The encoded protein, which may play a role in neuronal plasticity, is abundant in neurofibrillary lesions of patients with Alzheimer disease.
Synonyms
Beta-synuclein, SNCB, b-Synuclein.
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
MDVFMKGLSM AKEGVVAAAE KTKQGVTEAA EKTKEGVLYV GSKTREGVVQ GVASVAEKTK EQASHLGGAV FSGAGNIAAA TGLVKREEFP TDLKPEEVAQ EAAEEPLIEP LMEPEGESYE DPPQEEYQEY EPEA.

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:

Beta-2 Microglobulin Human

Beta-2-microglobulin, B2M.

Product # :

PRO-553

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Description

Human Beta-2 Microglobulin produced in Human urine from patients with tubular proteinuria having a molecular mass of 12KDa.

Source

Human urine from patients with tubular proteinuria.

Formulation

Lyophilized from 0.02M NH4HCO3 pH-7.2, 0.15M NaCl, 1mM EDTA, 2% mannitol and 0.09% NaN3.

Purity

Greater than 95%.

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Introduction
Beta 2 microglobulin is an 11 kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. Beta 2 microglobulin associates with class I-like molecules such as CD1 and Qa as well as with the alpha chain of MHC class I molecules. Very limited amounts of MHC class I molecules can be found on the surface in the absence of Beta 2 microglobulin. CD8 T cells cannot develop in the absence of MHC class I.
Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinaemia, renal failure, or kidney transplants. Human Beta 2 microglobulin levels can rise either because its rate of synthesis has increased (e.g. in AIDS, malignant monoclonal plasma cell dyscrasia, solid tumors and autoimmune disease) or because of impaired renal filtration (e.g. due to renal insufficiency, graft rejection or nephrotoxicity induced by post-transplantation immunosuppressive therapy). Beta-2 microglobulin levels might also be elevated in multiple myeloma and lymphoma cases. Dialysis-related amyloidosis develops after a long-term hemodialysis, it can aggregate into amyloid fibers that deposit in joint spaces.
Synonyms
Beta-2-microglobulin, B2M.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Human B2M although stable at room temperature for 3 weeks, should be stored between 2-8°C.
Solubility
It is recommended to reconstitute the lyophilized HuB2M in water at 1mg/ml.
Human Virus Test
Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen and Hepatitis C antibodies.

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 Factor, Augmenter of Liver Regeneration Human Recombinant

FAD-linked sulfhydryl oxidase ALR, Augmenter of liver regeneration, Hepatopoietin, GFER, ALR, HERV1, HPO, ALR, HSS, ERV1, HPO1, HPO2.

Product # :

PRO-1326

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Description

GFER Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-205 a.a) and having a molecular mass of 26kDa.GFER is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
FAD-linked sulfhydryl oxidase ALR (GFER) is a member of the Erv1/ALR family of proteins, which is found in higher and lower eukaryotes. GFER is a hepatotrophic growth factor and flavin-linked sulfhydryl oxidase expressed in a variety of tissues. Moreover, GFER induces the expression of S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases (ODC), which each have a central role in the synthesis of polyamines. The hepatotrophic factor designated augmenter of liver regeneration (ALR) is assumed to be one of the factors responsible for the exceptional regenerative capacity of mammalian liver. The GFER gene is located on chromosome 16 in the interval containing the locus for polycystic kidney disease (PKD1).
Synonyms
FAD-linked sulfhydryl oxidase ALR, Augmenter of liver regeneration, Hepatopoietin, GFER, ALR, HERV1, HPO, ALR, HSS, ERV1, HPO1, HPO2.
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 MGSHMAAPGE RGRFHGGNLF FLPGGARSEM MDDLATDARG RGAGRRDAAA SASTPAQAPT SDSPVAEDAS RRRPCRACVD FKTWMRTQQK RDTKFREDCP PDREELGRHS WAVLHTLAAY YPDLPTPEQQ QDMAQFIHLF SKFYPCEECA EDLRKRLCRN HPDTRTRACF TQWLCHLHNE VNRKLGKPDF DCSKVDERWR DGWKDGSCD.

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:

Beta 2 Microglobulin Human Recombinant, His Tag

Beta-2-microglobin, Beta chain of MHC class I molecules, B2M, Beta 2 Microglobulin.

Product # :

PRO-859

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Description

B2M Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (21-119 a.a.) and having a molecular mass of 14 kDa. The B2M is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

B2M Human solution containing 20mM Tris pH-8, 2mM DTT, 0.1M NaCl & 20% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
B2M is a part of the MHC class I family that participates in the presentation of peptide antigens to the immune system. B2M is localized on the surface of numerous cells and abundant on the surface of white blood cells. High production or destruction of these cells causes B2M levels in the blood to raise. This increase is observed in people with cancers involving white blood cells, but it is mainly significant in people newly diagnosed with multiple myeloma. B2M Testing is done primarily when evaluating a person for certain kinds of cancer affecting white blood cells including chronic lymphocytic leukemia, non-Hodgkin''s lymphoma, and multiple myeloma or kidney disease.
Synonyms
Beta-2-microglobin, Beta chain of MHC class I molecules, B2M, Beta 2 Microglobulin.
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 MIQRTPKIQV YSRHPAENGK SNFLNCYVSG FHPSDIEVDL LKNGERIEKV EHSDLSFSKD WSFYLLYYTE FTPTEKDEYA CRVNHVTLSQ PKIVKWDRDM.

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 15 Human Recombinant, His Tag

GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

Product # :

CYT-691

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Description

Recombinant Human GDF15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (195-308) and having a molecular mass of 16.7 kDa(molecular weight on SDS-PAGE will appear higher).GDF15 is expressed with a 36 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDF15 protein solution contains 10mM sodium citrate, pH-3.5 & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
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 KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.
Background
What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein has a total Mw of 16.7kDa.

What is the source or expression system of GDF15 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF15 HUMAN, HIS Protein?
The biological functionality of GDF15 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.

What applications can GDF15 HUMAN, HIS Protein be used in?
GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and
Lateral Flow.

What is the endotoxin level for GDF15 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF15 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:

Fibroblast Growth Factor-acidic Mouse Recombinant, His Tag

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Product # :

CYT-072

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sds-page

Description

FGF-1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (16-155 a.a) and having a molecular mass of 18kDa (Molecular weight on SDS-PAGE will appear higher).FGF-1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

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Introduction
Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Physical Appearance
Sterile Filtered colorless 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 MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 18kDa.

What is the source or expression system of FGF 1 Protein?
Escherichia Coli.

What is the Purity of FGF 1 Protein?
FGF 1 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 1 Protein?
The biological functionality of FGF 1 Protein will be determined in the future.

What is the amino acid sequence of FGF 1 Protein?
MGSSHHHHHH SSGLVPRGSH MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

What applications can FGF 1 Protein be used in?
FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 1 Protein?
The endotoxin level is minimal, FGF 1 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-acidic (154 a.a.) Human Recombinant

HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

Product # :

CYT-1112

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Shipped at Room temp

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Description

Fibroblast Growth Factor-acidic Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids and having a molecular mass of 17.3kDa. The FGF1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4, with 0.5mM DTT, 2mM EDTA, and 5 % Trehalose.

Purity

Greater than 97.0% as determined by:

(a) Analysis by RP-HPLC.

(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < than 0.5 ng/ml, corresponding to a specific activity of > 2.0 ×10⁶IU/mg in the presence of 10µg/ml Heparin.

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Introduction
Acidic fibroblast growth factor 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. FGF1 functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor.FGF1 acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Synonyms
HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor-acidic 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 Fibroblast Growth Factor-acidic Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AEGEITTFTA LTEKFNLPPG NYKKPKLLYC SNGGHFLRIL PDGTVDGTRD RSDQHIQLQL SAESVGEVYI KSTETGQYLA MDTDGLLYGS QTPNEECLFL ERLEENHYNT YISKKHAEKN WFVGLKKNGS CKRGPRTHYG QKAILFLPLP VSSD.
Background
What is the molecular weight/Mw of FGF 1 Protein?
FGF 1 Protein has a total Mw of 17.3kDa.

What is the source or expression system of FGF 1 Protein?
Escherichia Coli.

What is the Purity of FGF 1 Protein?
FGF 1 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 1 Protein?
The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < than 0.5 ng/ml, corresponding to a specific activity of > 2.0 ×106 IU/mg in the presence of 10µg/ml Heparin.

What is the amino acid sequence of FGF 1 Protein?
AEGEITTFTA LTEKFNLPPG NYKKPKLLYC SNGGHFLRIL PDGTVDGTRD RSDQHIQLQL SAESVGEVYI KSTETGQYLA MDTDGLLYGS QTPNEECLFL ERLEENHYNT YISKKHAEKN WFVGLKKNGS CKRGPRTHYG QKAILFLPLP VSSD.

What applications can FGF 1 Protein be used in?
FGF 1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF 1 Protein?
The endotoxin level is minimal, FGF 1 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:

Beta-1,3-Glucuronyltransferase 3 Human Recombinant

Beta-1,3-glucuronyltransferase 3, GLCATI, Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3, UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase.

Product # :

ENZ-711

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Description

B3GAT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (29-335 a.a) and having a molecular mass of 36.4kDa. B3GAT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

B3GAT3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Beta-1,3-glucuronyltransferase 3 (B3GAT3) is involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. B3GAT3 has a part in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. B3GAT3 shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc.
Synonyms
Beta-1,3-glucuronyltransferase 3, GLCATI, Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3, UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase.
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 MGSQPCDCLP PLRAAAEQLR QKDLRISQLQ AELRRPPPAP AQPPEPEALP TIYVVTPTYA RLVQKAELVR LSQTLSLVPR LHWLLVEDAE GPTPLVSGLL AASGLLFTHL VVLTPKAQRL REGEPGWVHP RGVEQRNKAL DWLRGRGGAV GGEKDPPPPG TQGVVYFADD DNTYSRELFE EMRWTRGVSV WPVGLVGGLR FEGPQVQDGR VVGFHTAWEP SRPFPVDMAG FAVALPLLLD KPNAQFDSTA PRGHLESSLL SHLVDPKDLE PRAANCTRVL VWHTRTEKPK MKQEEQLQRQ GRGSDPAIEV.

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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