Search: 1000 results found for "pleiotrophin"

Description:

Fibroblast Growth Factor-5 Human Recombinant

Fibroblast Growth Factor 5, Heparin-Binding Growth Factor 5, Smag-82, HBGF-5, TCMGLY, FGF-5, FGF5.

Product # :

CYT-957

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Description

FGF5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain having containing 252 amino acids and having a molecular mass of 27.7kDa.The FGF-5 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGF-5 protein was lyophilized from a 0.2µm filtered solution in 10mM sodium phosphate and 100mM sodium chloride pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Fibroblast Growth Factor-5 (FGF5) belongs to the FGF family of mitogenic peptides. In vitro, rhFGF5 is a mitogen for Balb/3T3 fibroblasts and bovine heart endothelial cells. FGF5 is also a major muscle-derived survival factor for cultured spinal motoneurons. In vivo, FGF5 is assumed to play central roles in both embryology and neurobiology. Developmentally, FGF5 mRNA is originally found in the embryoblast followed by the lateral somatic mesoderm, where it may play a part in angiogenesis, as well as the myotomes cranial to the tail region, where it may delay terminal myoblast differentiation during cell migration.
Synonyms
Fibroblast Growth Factor 5, Heparin-Binding Growth Factor 5, Smag-82, HBGF-5, TCMGLY, FGF-5, FGF5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-5 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 FGF5 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAWAHGEKRL APKGQPGPAA TDRNPRGSSS RQSSSSAMSS SSASSSPAAS LGSQGSGLEQ SSFQWSPSGR RTGSLYCRVG IGFHLQIYPD GKVNGSHEAN MLSVLEIFAV SQGIVGIRGV FSNKFLAMSK KGKLHASAKF TDDCKFRERF QENSYNTYAS AIHRTEKTGR EWYVALNKRG KAKRGCSPRV KPQHISTHFL PRFKQSEQPE LSFTVTVPEK KKPPSPIKSK IPLSAPRKNT NSVKYRLKFR FG.
Background
What is the molecular weight/Mw of FGF5 HUMAN Protein?
FGF5 HUMAN Protein has a total Mw of 27.7kDa.

What is the source or expression system of FGF5 HUMAN Protein?
Escherichia Coli.

What is the Purity of FGF5 HUMAN Protein?
FGF5 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF5 HUMAN Protein?
The biological functionality of FGF5 HUMAN Protein will be determined in the future.

What is the amino acid sequence of FGF5 HUMAN Protein?
MAWAHGEKRL APKGQPGPAA TDRNPRGSSS RQSSSSAMSS SSASSSPAAS LGSQGSGLEQ SSFQWSPSGR RTGSLYCRVG IGFHLQIYPD GKVNGSHEAN MLSVLEIFAV SQGIVGIRGV FSNKFLAMSK KGKLHASAKF TDDCKFRERF QENSYNTYAS AIHRTEKTGR EWYVALNKRG KAKRGCSPRV KPQHISTHFL PRFKQSEQPE LSFTVTVPEK KKPPSPIKSK IPLSAPRKNT NSVKYRLKFR FG.
What applications can FGF5 HUMAN Protein be used in?
FGF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF5 HUMAN Protein?
The endotoxin level is minimal, FGF5 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:

Osteoprotegerin Human Recombinant /Fc Chimera

TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

Product # :

CYT-266

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Description

Recombinant OPG produced in yeast contains 2x412 amino acid residues, including 180 residues from mature OPG (a.a 22-201) and 232 residues from the Fc protein of human IgG1, and has a calculated molecular mass of 109.6kDa.

Source

Pichia Pastoris.

Formulation

OPG was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 6.0, 150mM NaCl and 0.02 % Tween-80.

Purity

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

Biological Activity

The ED₅₀ as determined by neutralizing the stimulation of U937 cells is less tha10ng/ml, corresponding to a specific activity of > 1.0 × 10⁵IU/mg in the presence of 10ng/ml soluble Human RANKL (sRANKL).

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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Osteoprotegerin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OCIF 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 Osteoprotegerin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
OPG 22-201 ETFPPKYLHY DEETSHQLLC DKCPPGTYLK QHCTAKWKTV CAPCPDHYYT DSWHTSDECL YCSPVCKELQ YVKQECNRTH NRVCECKEGR YLEIEFCLKH RSCPPGFGVV QAGTPERNTV CKRCPDGFFS NETSSKAPCR KHTNCSVFGL LLTQKGNATH DNICSGNSES TQKCGIDVTL
Fc232EPKSSDKTHT CPPCPAPEFE GAPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPTPIEKTISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK

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

Description:

Bone Morphogenetic protein-3 Human Recombinant

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

Product # :

CYT-937

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

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

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

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

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

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

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

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

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

Description:

Fibroblast Growth Factor-23 Human Recombinant, Sf9

Fibroblast growth factor 23, FGF-23, Phosphatonin, Tumor-derived hypophosphatemia-inducing factor, HYPF.

Product # :

CYT-1102

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Description

FGF23 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 236 amino acids (25-251a.a.) and having a molecular mass of 26.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).FGF23 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

FGF23 protein solution (0.25mg/ml) containsPhosphate Buffered Saline (pH 7.4), 2mM DTT, 1mM EDTA and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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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, tissue repair, morphogenesis, 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. a high level expression of FGF23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism.
Synonyms
Fibroblast growth factor 23, FGF-23, Phosphatonin, Tumor-derived hypophosphatemia-inducing factor, HYPF.
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
ADPYPNASPL LGSSWGGLIH LYTATARNSY HLQIHKNGHV DGAPHQTIYS ALMIRSEDAG
FVVITGVMSR RYLCMDFRGN IFGSHYFDPE NCRFQHQTLE NGYDVYHSPQ YHFLVSLGRA
KRAFLPGMNP PPYSQFLSRR NEIPLIHFNT PIPRRHTRSA EDDSERDPLN VLKPRARMTP
APASCSQELP SAEDNSPMAS DPLGVVRGGR VNTHAGGTGP EGCRPFAKFI HHHHHH.
Background
What is the molecular weight/Mw of FGF23 HUMAN, SF9 Protein?
FGF23 HUMAN, SF9 Protein has a total Mw of 26.4kDa.

What is the source or expression system of FGF23 HUMAN, SF9 Protein?
Sf9, Insect cells.
What is the Purity of FGF23 HUMAN, SF9 Protein?
FGF23 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF23 HUMAN, SF9 Protein?
The biological functionality of FGF23 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of FGF23 HUMAN, SF9 Protein?
ADPYPNASPL LGSSWGGLIH LYTATARNSY HLQIHKNGHV DGAPHQTIYS ALMIRSEDAG
FVVITGVMSR RYLCMDFRGN IFGSHYFDPE NCRFQHQTLE NGYDVYHSPQ YHFLVSLGRA
KRAFLPGMNP PPYSQFLSRR NEIPLIHFNT PIPRRHTRSA EDDSERDPLN VLKPRARMTP
APASCSQELP SAEDNSPMAS DPLGVVRGGR VNTHAGGTGP EGCRPFAKFI HHHHHH.
What applications can FGF23 HUMAN, SF9 Protein be used in?
FGF23 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF23 HUMAN, SF9 Protein?
The endotoxin level is minimal, FGF23 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

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

Description:

Melanoma Antigen Family D, 1 Human Recombinant

MAGED1, Melanoma Antigen Family D 1, Neurotrophin Receptor-Interacting, MAGE Homolog, NRAGE, MAGE Tumor Antigen CCF, MAGE-D1 Antigen, DLXIN-1, Melanoma-Associated Antigen D1.

Product # :

PRO-1796

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Description

MAGED1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 280 amino acids (504-760 a.a) and having a molecular mass of 31.7kDa.MAGED1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

MAGED1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Melanoma-associated antigen D1 (MAGED1) belongs to the melanoma antigen gene (MAGE) family and expressed in virtually all normal adult tissues. MAGED1 is involved in the p75 neurotrophin receptor mediated programmed cell death pathway. MAGED1 is involved in Prader-Willi syndrome including hyperphagia, repetitive and compulsive behaviors, and cognitive impairment. MAGED1 is involved in the apoptotic response following NGF (nerve growth factor) binding in neuronal cells. MAGED1 hinders cell cycle progression, and facilitates NGFR-mediated apoptosis. MAGED1 functions as a regulator of the function of DLX family members. MAGED1 has a role in the circadian rythm regulation.
Synonyms
MAGED1, Melanoma Antigen Family D 1, Neurotrophin Receptor-Interacting, MAGE Homolog, NRAGE, MAGE Tumor Antigen CCF, MAGE-D1 Antigen, DLXIN-1, Melanoma-Associated Antigen D1.
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 MGSLRPSPNS RASQNPGAAQ PRDVALLQER ANKLVKYLML KDYTKVPIKR SEMLRDIIRE YTDVYPEIIE RACFVLEKKF GIQLKEIDKE EHLYILISTP ESLAGILGTT KDTPKLGLLL VILGVIFMNG NRASEAVLWE ALRKMGLRPG VRHPLLGDLR KLLTYEFVKQ KYLDYRRVPN SNPPEYEFLW GLRSYHETSK MKVLRFIAEV QKRDPRDWTA QFMEAADEAL DALDAAAAEA EARAEARTRM GIGDEAVSGP.

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:

Natriuretic Peptide A Human Recombinant

Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.

Product # :

CYT-1028

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Description

NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).

Source

Escherichia Coli.

Formulation

NPPA filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Natriuretic Peptide A (NPPA) is a part of the natriuretic peptide family and is involved in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. NPPA is synthesized as a great precursor which releases a peptide from the N-terminus with similarity to vasoactive peptide, cardiodilatin, and another peptide from the C-terminus with natriuretic-diuretic activity. In female pregnancy, NPPA is promoting trophoblast invasion and spiral artery remodeling in uterus.
Synonyms
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
Physical Appearance
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; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. NPPA is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHNP MYNAVSNADL MDFKNLLDHL EEKMPLEDEV VPPQVLSEPN EEAGAALSPL PEVPPWTGEV SPAQRDGGAL GRGPWDSSDR SALLKSKLRA LLTAPR.

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 (1-51 a.a.)Human Recombinant

Urogastrone, URG, EGF.

Product # :

CYT-1115

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Description

Epidermal Growth Factor (1-51 a.a.) Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 6.0kDa. The EGF is purified by proprietary chromatographic techniques.

Source

Saccharomyces cerevisiae

Formulation

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

The ED50 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 10⁷ IU/mg.

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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 several epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epidermal Growth Factor 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 Epidermal 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
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.
Background
Exploring the Potential of Epidermal Growth Factor (1-51 a.a.) Human Recombinant: Novel Insights and Therapeutic Prospects
Abstract:
Epidermal Growth Factor (EGF) stands as a pivotal cytokine orchestrating essential cellular processes. This concise research paper delves into the unique realm of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, unveiling its intricate molecular dynamics, signaling cascades, and therapeutic promise. Employing cutting-edge methodologies encompassing in vitro assays and animal models, this study elucidates the multifaceted cellular responses sparked by this truncated EGF variant, paving the way for potential clinical applications.
Introduction:
The truncated form of EGF, spanning amino acids 1 to 51 (a.a.), carries distinct attributes that set it apart from the full-length counterpart. This paper centers on exploring the intriguing dimensions of Epidermal Growth Factor (1-51 a.a.) Human Recombinant, offering new insights into its interactions and potential utility.
Molecular Insights and Signaling Dynamics:
At the heart of its function lies the interplay between EGF (1-51 a.a.) and the epidermal growth factor receptor (EGFR). High-resolution structural analyses unveil the nuances of their binding interface, initiating a cascade of phosphorylation events that trigger canonical and non-canonical signaling pathways. The MAPK pathway and the PI3K/Akt pathway, intricately modulated by EGF (1-51 a.a.), propel cellular processes like proliferation, migration, and evasion of apoptosis.
In Vitro Profiling and Cellular Responses:
In dissecting the cellular responses, diverse in vitro assays have been employed. These encompass cell viability assays, wound healing assays, and intricate fluorescence resonance energy transfer (FRET) studies. These assays converge to illuminate the dynamic orchestration of EGF-induced cellular behaviors, showcasing its role in promoting cellular migration, division, and wound closure.
In Vivo Implications and Therapeutic Horizons:
Translating these insights into tangible therapeutic possibilities, in vivo studies present a compelling narrative. In animal models, EGF (1-51 a.a.) emerges as a potent player in cutaneous wound healing, fostering accelerated tissue regeneration. Moreover, its potential extends to oncology, as it not only influences tumor microenvironments but also demonstrates anti-apoptotic effects, hinting at its role in tailored cancer interventions.
Future Prospects and Challenges:
While these discoveries hold immense promise, challenges persist. The intricate network of signaling events demands further scrutiny, considering potential cross-talk and off-target effects. Refining delivery mechanisms and dosing regimens is essential for realizing the clinical potential of EGF (1-51 a.a.).
Conclusion:
In a synthesis of complex molecular insights and tangible therapeutic potential, Epidermal Growth Factor (1-51 a.a.) Human Recombinant emerges as a captivating subject. Its truncated structure and distinctive signaling cascades paint a canvas of cellular orchestration. As research advances, harnessing its therapeutic benefits could usher in novel interventions for wound healing and cancer therapy.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6kDa.

What is the source or expression system of EGF Protein?
Saccharomyces cerevisiae

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

What is the Biological Activity of EGF Protein?
The ED50 is determined by a cell proliferation assay using murine Balb/c 3T3 cells and is < than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107 IU/mg.

What is the amino acid sequence of EGF Protein?
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

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

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

Erythropoietin Rat Recombinant

Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.

Product # :

CYT-1187

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Description

EPO Rat Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-192 a.a) containing 175 amino acids and having a molecular mass of 19.6 kDa. EPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

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Introduction
Erythropoietin or EPO is a hormone (glycoprotein), part of the type I cytokine group of proteins. EPO is found mainly in the kidney tissue, produced from fibroblast-like cortical interstitial cells near the proximal tubules. EPO is also present in the blood, where it acts as red cell production regulator, by the promotion of differentiation of erythroid and thereby starts hemoglobin synthesis. Furthermore, EPO has neuroprotective activity towards brain injuries & anti-apoptotic activity in different tissues.
Synonyms
Erythropoietin-Alpha, EPO-a, EPO-alpha, EP, MGC138142.
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
DGSAPPRLIC DSRVLERYIL EAKEAENVTM GCAEGPRLSE NITVPDTKVN FYAWKRMKVE EQAVEVWQGL SLLSEAILQA QALQANSSQP PESLQLHIDK AISGLRSLTS LLRVLGAQKE LMSPPDATQA APLRTLTADT FCKLFRVYSN FLRGKLKLYT GEACRRGDRH HHHHH.
Background
What is the molecular weight/Mw of EPO Protein?
EPO Protein has a total Mw of 19.6kDa.

What is the source or expression system of EPO Protein?
HEK293 cells.

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

What is the Biological Activity of EPO Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.

What is the amino acid sequence of EPO Protein?
DGSAPPRLIC DSRVLERYIL EAKEAENVTM GCAEGPRLSE NITVPDTKVN FYAWKRMKVE EQAVEVWQGL SLLSEAILQA QALQANSSQP PESLQLHIDK AISGLRSLTS LLRVLGAQKE LMSPPDATQA APLRTLTADT FCKLFRVYSN FLRGKLKLYT GEACRRGDRH HHHHH.

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

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

Oncostatin-M Human Recombinant (195 a.a.)

OSM, MGC20461, Oncostatin M.

Product # :

CYT-735

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Description

Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids and having a molecular mass of 22kDa. The OSM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 1xPBS pH-7.4.

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 the dose-dependent stimulation of the proliferation of human TF-1 cells is < 0.2ng/ml, corresponding to a specific activity of > 5.0x10⁶ units/mg.

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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
Synonyms
OSM, MGC20461, Oncostatin M.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSR.

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:

Phosphodiesterase 6H cGMP-Specific Cone Gamma Human Recombinant

Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.

Product # :

ENZ-819

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Description

PDE6H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 106 amino acids (1-83 a.a) and having a molecular mass of 11.5 kDa. PDE6H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PDE6H protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol, 2mM DTT and 0.1mM PMSF.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
PDE6H belongs to the rod/cone cGMP-PDE gamma subunit family, which selectively catalyze the hydrolysis of 3 cyclic phosphate bonds in adenosine and/or guanine 3,5 cyclic monophosphate (cAMP and/or cGMP). This family regulates the cellular levels, localization and duration of action of these second messengers by controlling the rate of their degradation. PDE6H is the inhibitory (or gamma) subunit of the cone-specific cGMP phosphodiesterase, which is atetramer composed of two catalytic chains (alpha and beta), and two inhibitory chains (gamma). PDE6H is particularly expressed in the retina, and is implicated in the transmission and amplification of the visual signal. Mutations in PDE6H have been associated with retinal cone dystrophy type 3A.
Synonyms
Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.
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 MGSMSDNTTL PAPASNQGPT TPRKGPPKFK QRQTRQFKSK PPKKGVKGFG DDIPGMEGLG TDITVICPWE AFSHLELHEL AQFGII.

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:

Prefoldin Subunit 6 Human Recombinant

Prefoldin Subunit 6, PFD6, H2-KE2, KE-2, HKE2, HLA class II region expressed gene KE2, MGC70744.

Product # :

PRO-178

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Description

PFDN6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids (1-129a.a.) and having a molecular mass of 16.7 kDa. PFDN6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PFDN6 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
PFDN6 is a subunit of the heteromeric prefoldin complex that chaperones developing actin and alpha- and beta-tubulin chains until they are transferred to the cytosolic chaperonin containing TCP1 (CCT) complex. PFDN6 binds specifically to cytosolic chaperonin (c-CPN), transfers target proteins to it and bind to developing polypeptide chain to promote folding in a setting where there are many competing pathways for nonnative proteins.
Synonyms
Prefoldin Subunit 6, PFD6, H2-KE2, KE-2, HKE2, HLA class II region expressed gene KE2, MGC70744.
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 MAELIQKKLQ GEVEKYQQLQ KDLSKSMSGR QKLEAQLTEN NIVKEELALL DGSNVVFKLL GPVLVKQELG EARATVGKRL DYITAEIKRY ESQLRDLERQ SEQQRETLAQ LQQEFQRAQA AKAGAPGKA

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:

Proline-Rich Acidic Protein 1 Human Recombinant

Proline-rich acidic protein 1, Epididymis tissue protein Li 178, Uterine-specific proline-rich acidic protein, PRAP1, UPA, PRO1195.

Product # :

PRO-1598

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Description

PRAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 21-151) containing 141 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 16.2kDa (calculated).

Source

Escherichia Coli.

Formulation

PRAP1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Proline-rich acidic protein 1 (PRAP1) is essential for maintaining homeostasis in epithelial cells e.g. in liver or gastrointestinal tract. PRAP1 is abundantly expressed in the epithelial cells of the liver, kidney, gastrointestinal tract and cervix. PRAP1 is notably down-regulated in hepatocellular carcinoma and right colon adenocarcinoma compared with the respective adjacent normal tissues.
Synonyms
Proline-rich acidic protein 1, Epididymis tissue protein Li 178, Uterine-specific proline-rich acidic protein, PRAP1, UPA, PRO1195.
Physical Appearance
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; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. PRAP1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASVPAPKVPIKM QVKHWPSEQD PEKAWGARVV EPPEKDDQLV VLFPVQKPKL LTTEEKPRGQ GRGPILPGTK AWMETEDTLG HVLSPEPDHD SLYHPPPEED QGEERPRLWV MPNHQVLLGP EEDQDHIYHP Q.

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 (121) Human Recombinant, HEK

Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

Product # :

CYT-116

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Description

Recombinant Human VEGF 121 amino acids, produced in HEK cells is a glycosylated 37kDa homodimer and 50kDa homotrimer.The VEGF is purified by proprietary chromatographic techniques.

Source

HEK.

Formulation

VEGF was lyophilized from a 0.2µm filtered solution containing 1xPBS.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

The specific activity was determined by the dose-dependent stimulation of the proliferation of HUVEC cells (Human Umbilical Vein Endothelial Cells), the ED₅₀ is 3ng/ml.

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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF 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 VEGF in sterile PBS containing 0.1% endotoxin-free recombinant HSA.

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

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

Product # :

CYT-528

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Description

Fibroblast Growth Factor-acidic Mouse Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids and having a molecular mass of 15.9kDa. The FGF acidic is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.0, 5% Trehalose, 0.02% Tween-80, 0.5mM DTT and 0.5mM EDTA.

Purity

Greater than 96.0% as determined by SDS-PAGE and HPLC analyses.

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5x10⁶IU/mg.

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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 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 Fibroblast Growth Factor-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-a 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 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
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 15.9kDa.

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 >96% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF 1 Protein?
The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

What is the amino acid sequence of FGF 1 Protein?
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:

Transforming Growth Factor Beta 2 Human Recombinant

Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

Product # :

CYT-441

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Description

TGFB2 Human Recombinant produced in plants is a homodimeric polypeptide chain containing 2 x 118 amino acids and having a total molecular mass of 27.08kDa. The TGFB2 is fused to 6xHis Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Nicotiana benthamiana.

Formulation

Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The biological activity of TGFB2 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 < 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

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Introduction
TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-β (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.
Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB2 Human 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 TGFB2 in sterile 18M-cm H2O not less than 1µg/40µl, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HHHHHHALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIH
EPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASAS
PCCVSQDLEPLTI LYYIGKTPKIEQLSNMIVKSCKCS.

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 1 Human Recombinant

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.

Product # :

CYT-716

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Description

TGFB1 Human Recombinant produced in CHO cells is a glycosylated homodimeric polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa. The TGFB1 is purified by proprietary chromatographic techniques.

Source

CHO cells.

Formulation

Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA) And trehalose (1:20 protein to Trehalose ratio).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is 0.142ng/ml, corresponding to a specific activity of 7.4x10⁶units/mg.

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Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each 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.
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 Human 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 TGFB1 in sterile 10mM HCl at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDTNYCFSS TEKNCCVRQL YIDFRKDLGW KWIHEPKGYH ANFCLGPCPY IWSLDTQYSK VLALYNQHNP GASAAPCCVP QALEPLPIVY YVGRKPKVEQ LSNMIVRSCK CS.
Background
Title: Transforming Growth Factor-Beta 1 Human Recombinant: A Promising Tool for Biomedical Research
Abstract:

Transforming Growth Factor-Beta 1 (TGF-β1) is a crucial cytokine involved in diverse cellular processes. This research paper provides an in-depth analysis of human recombinant TGF-β1, focusing on its production, purification, and applications in biomedical research. The paper discusses the significance of TGF-β1 in tissue engineering, regenerative medicine, and immunology. Furthermore, it elucidates the potential therapeutic implications of recombinant TGF-β1 in various diseases and highlights ongoing research in the field. The information presented in this paper aims to enhance the understanding of TGF-β1 and its utility as a research tool in biomedical sciences.
Introduction:

Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that regulates cellular processes such as cell growth, differentiation, and immune modulation. Human recombinant TGF-β1 is synthesized using genetic engineering techniques, enabling the production of large quantities of biologically active protein for research purposes.
Production and Purification:

Recombinant TGF-β1 is typically produced in expression systems such as bacteria, yeast, or mammalian cells. The protein is then purified using various chromatographic techniques to obtain a highly pure and active form. Quality control measures ensure the biological activity and integrity of the recombinant protein.
Biomedical Applications:

Human recombinant TGF-β1 has found broad applications in biomedical research. In tissue engineering and regenerative medicine, it plays a critical role in promoting cell proliferation, extracellular matrix production, and tissue repair. TGF-β1 is also involved in immune modulation, influencing immune cell differentiation and function. Recombinant TGF-β1 is a valuable tool for studying these processes and developing therapeutic interventions.
Therapeutic Implications:

The dysregulation of TGF-β1 signaling is associated with various diseases, including fibrosis, cancer, and autoimmune disorders. Recombinant TGF-β1 offers potential therapeutic applications through its ability to modulate cellular responses. Ongoing research aims to develop targeted therapies that specifically regulate TGF-β1 signaling for the treatment of these conditions.
Conclusion:

Human recombinant TGF-β1 holds immense potential as a research tool in biomedical sciences. Its production, purification, and applications in tissue engineering, regenerative medicine, and immunology contribute to advancing our understanding of cellular processes and disease mechanisms. With ongoing research, recombinant TGF-β1 may pave the way for novel therapeutic strategies in various medical fields.

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:

Aminoadipate-Semialdehyde Dehydrogenase-Phosphopantetheinyl Transferase Human Recombinant

L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase, 4'-phosphopantetheinyl transferase, Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase, AASD-PPT, LYS5 ortholog, AASDHPPT, LYS2, LYS5, CGI-80, DKFZp566E2346.

Product # :

ENZ-008

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Description

AASDHPPT Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 316 amino acids (14-309 a.a.) and having a molecular mass of 36.4kDa. The AASDHPPT is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The AASDHPPT solution (1mg/ml) contains 20mM 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
AASDHPPT is a member of the P-Pant transferase superfamily. AASDHPPT catalyzes the post-translational modification of target proteins by phosphopantetheine and can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN (in vitro). AASDHPPT is similar to Saccharomyces cerevisiae LYS5, which is required for the activation of the alpha-aminoadipate dehydrogenase in the biosynthetic pathway of lysine. AASDHPPT is found in the heart, skeletal muscle, placenta, testis, brain, pancreas, liver and kidney. It’s been suggested that defects in the human AASDHPPT gene result in pipecolic acidemia.
Synonyms
L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase, 4'-phosphopantetheinyl transferase, Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase, AASD-PPT, LYS5 ortholog, AASDHPPT, LYS2, LYS5, CGI-80, DKFZp566E2346.
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 MEGVRWAFSC GTWLPSRAEW LLAVRSIQPE EKERIGQFVF ARDAKAAMAG RLMIRKLVAE KLNIPWNHIR LQRTAKGKPV LAKDSSNPYP NFNFNISHQG DYAVLAAEPE LQVGIDIMKT SFPGRGSIPE FFHIMKRKFT NKEWETIRSF KDEWTQLDMF YRNWALKESF IKAIGVGLGF ELQRLEFDLS PLNLDIGQVY KETRLFLDGE EEKEWAFEES KIDEHHFVAV ALRKPDGSRH QDVPSQDDSK PTQRQFTILN FNDLMSSAVP MTPEDPSFWD CFCFTEEIPI RNGTKS.

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:

Eukaryotic Translation Elongation Factor 1 Alpha 1 Human Recombinant

Eukaryotic Translation Elongation Factor 1 Alpha 1, EF1A, EEF1A, LENG7, Leukocyte Receptor Cluster (LRC) Member 7, Elongation Factor Tu, Eukaryotic Elongation Factor 1 A-1, Leukocyte Receptor Cluster Member 7, EF-1-alpha-1, EF-Tu, eEF1A-1, CCS-3, CCS3, EE1A1, EEF-1, GRAF-1EF, HNGC:16303, PTI1, Cervical Cancer Suppressor 3, CTCL Tumor Antigen, EF1a-Like Protein, Elongation Factor 1 Alpha Subunit, Elongation Factor 1-Alpha 1, Eukaryotic Translation Elongation Factor 1 Alpha 1-Like 14, Glucocorticoid Receptor AF-1 Specific Elongation Factor, Prostate Tumor-Inducing Protein 1, Translation Elongation Factor 1 Alpha 1-Like 14.

Product # :

PRO-1910

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Description

EEF1A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (1-462 a.a) and having a molecular mass of 50kDa.

Source

Escherichia Coli.

Formulation

EEF1A1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
EEF1A1 is an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible forthe enzymatic release of aminoacyl tRNAs to the ribosome. EEF1A1 is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. EEF1A1 is recognized as an autoantigen in 66% of patients with Felty syndrome. EEF1A1 has multiple copies on numerous chromosomes, part of them, if not all, symbolize different pseudogenes. Among the diseases associated with EEF1A1 are tinea nigra and andcervical cancer.
Synonyms
Eukaryotic Translation Elongation Factor 1 Alpha 1, EF1A, EEF1A, LENG7, Leukocyte Receptor Cluster (LRC) Member 7, Elongation Factor Tu, Eukaryotic Elongation Factor 1 A-1, Leukocyte Receptor Cluster Member 7, EF-1-alpha-1, EF-Tu, eEF1A-1, CCS-3, CCS3, EE1A1, EEF-1, GRAF-1EF, HNGC:16303, PTI1, Cervical Cancer Suppressor 3, CTCL Tumor Antigen, EF1a-Like Protein, Elongation Factor 1 Alpha Subunit, Elongation Factor 1-Alpha 1, Eukaryotic Translation Elongation Factor 1 Alpha 1-Like 14, Glucocorticoid Receptor AF-1 Specific Elongation Factor, Prostate Tumor-Inducing Protein 1, Translation Elongation Factor 1 Alpha 1-Like 14.
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
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GNASGTTLLE ALDCILPPTR PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK ITKSAQKAQK AK

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:

Ephrin A1 Human Recombinant

Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

Product # :

PRO-971

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Description

EFNA1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (19-182) and having a molecular mass of 21.6 kDa.EFNA1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The EFNA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.
Synonyms
Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.
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 MDRHTVFWNS SNPKFRNEDY TIHVQLNDYV DIICPHYEDH SVADAAMEQY ILYLVEHEEY QLCQPQSKDQ VRWQCNRPSA KHGPEKLSEK FQRFTPFTLG KEFKEGHSYY YISKPIHQHE DRCLRLKVTV SGKITHSPQA HVNPQEKRLA ADDPEVRVLH SIGHS

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:

Ephrin A5 Human Recombinant

EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.

Product # :

PRO-2327

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Description

EFNA5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 422 amino acids (21-203 a.a.) and having a molecular mass of 48.1kDa. EFNA5 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

EFNA5 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Ephrin A5 (EFNA5) is a part of the ephrin ligand family which binds the members of ephrin receptor subfamily of tyrosine kinases and stimulates contact-dependent bidirectional signaling into neighboring cells. EFNA5 is mainly expressed in human adult brain, heart, spleen, and ovary and human fetal brain, lung, and kidney.
Synonyms
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
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
QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR GENLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

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-8b Human Recombinant

Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.

Product # :

CYT-830

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Description

BMP8B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (264-402a.a.) and having a molecular mass of 18.1kDa.BMP8B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

BMP8B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Bone Morphogenetic protein-8b (BMP8B) belongs to a family of secreted signaling molecules which can induce ectopic bone growth. BMP8B is known for having a possible bone inductive activity as it is related to BMP5 and BMP7. BMP8B is the osteoinductive factor accountable for epithelial osteogenesis.
Synonyms
Bone morphogenetic protein 8B, BMP-8, BMP-8B, Osteogenic protein 2, OP-2, BMP8B, BMP8, Bone Morphogenetic protein-8b, OP2.
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 MGSAVRPLRR RQPKKSNELP QANRLPGIFD DVHGSHGRQV CRRHELYVSF QDLGWLDWVI APQGYSAYYC EGECSFPLDS CMNATNHAIL QSLVHLMMPD AVPKACCAPT KLSATSVLYY DSSNNVILRK HRNMVVKACG CH.
Background
Bone Morphogenetic Protein-8B Human Recombinant: Unveiling the Potential for Regenerative Medicine and Tissue Engineering
Abstract:
Bone Morphogenetic Protein-8B (BMP-8B) human recombinant is a key member of the bone morphogenetic protein family, renowned for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-8B, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-8B human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine and tissue engineering.
Introduction:
Regenerative medicine and tissue engineering offer promising solutions to address the challenges of tissue repair and regeneration. BMP-8B, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper delves into the distinctive features of BMP-8B and presents novel approaches for the production and optimization of BMP-8B human recombinant, aiming to unleash its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-8B 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, thereby initiating intricate intracellular signaling cascades. BMP-8B signaling pathways, including Smad-dependent and Smad-independent pathways, regulate crucial processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.
Production of BMP-8B Human Recombinant:
Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-8B 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-8B. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-8B recombinant protein.
Potential Therapeutic Applications:
BMP-8B human recombinant holds immense promise in the field of regenerative medicine and tissue engineering. Its involvement in bone and cartilage formation, muscle regeneration, and wound healing makes it a potential candidate for the treatment of skeletal disorders, muscle injuries, and chronic wounds. Furthermore, the ability of BMP-8B to modulate cell behavior and tissue remodeling highlights its broader therapeutic applications in diverse regenerative processes.
Conclusion:
BMP-8B human recombinant emerges as a crucial regulator in regenerative medicine and tissue engineering, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. Given its involvement in bone, cartilage, and muscle formation, as well as wound healing, BMP-8B 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 BMP8B Protein?
BMP8B Protein has a total Mw of 18.1kDa.

What is the source or expression system of BMP8B Protein?
Escherichia Coli.

What is the Purity of BMP8B Protein?
BMP8B Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP8B Protein?
The biological functionality of BMP8B Protein will be determined in the future.

What is the amino acid sequence of BMP8B Protein?
MGSSHHHHHH SSGLVPRGSH MGSAVRPLRR RQPKKSNELP QANRLPGIFD DVHGSHGRQV CRRHELYVSF QDLGWLDWVI APQGYSAYYC EGECSFPLDS CMNATNHAIL QSLVHLMMPD AVPKACCAPT KLSATSVLYY DSSNNVILRK HRNMVVKACG CH.

What applications can BMP8B Protein be used in?
BMP8B Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP8B Protein?
The endotoxin level is minimal, BMP8B 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:

Parvin Alpha Human Recombinant

Alpha-parvin, Actopaxin, CH-ILKBP, Calponin-like integrin-linked kinase-binding protein, Matrix-remodeling-associated protein 2, PARVA, MXRA2.

Product # :

PRO-1257

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Description

PARVA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 395 amino acids (1-372 a.a) and having a molecular mass of 44.6kDa.PARVA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PARVA protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Alpha-parvin (PARVA) belongs to the parvin family of actin-binding proteins. PARVA has a role in the regulation of cell adhesion, cytoskeleton organization, motility and survival as well as in ciliogenesis. Parvins are related with focal contacts and contain calponin homology domains which connect to actin filaments. PARVA is extensively expressed, with the highest levels in heart, skeletal muscle, kidney and liver.
Synonyms
Alpha-parvin, Actopaxin, CH-ILKBP, Calponin-like integrin-linked kinase-binding protein, Matrix-remodeling-associated protein 2, PARVA, MXRA2.
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 MGSMATSPQK SPSVPKSPTP KSPPSRKKDD SFLGKLGGTL ARRKKAKEVS ELQEEGMNAI NLPLSPIPFE LDPEDTMLEE NEVRTMVDPN SRSDPKLQEL MKVLIDWIND VLVGERIIVK DLAEDLYDGQ VLQKLFEKLE SEKLNVAEVT QSEIAQKQKL QTVLEKINET LKLPPRSIKW NVDSVHAKSL VAILHLLVAL SQYFRAPIRL PDHVSIQVVV VQKREGILQS RQIQEEITGN TEALSGRHER DAFDTLFDHA PDKLNVVKKT LITFVNKHLN KLNLEVTELE TQFADGVYLV LLMGLLEGYF VPLHSFFLTP DSFEQKVLNV SFAFELMQDG GLEKPKPRPE DIVNCDLKST LRVLYNLFTK YRNVE.

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:

Placental Lactogen Ovine Recombinant

Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

Product # :

CYT-512

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Description

Placental Lactogen Ovine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

Purity

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

Biological Activity

Placental Lactogen Ovine is biologically active as evidenced by inducing proliferation of Nb2 cells.

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Introduction
Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
Placental Lactogen Ovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.
Synonyms
Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Placental Lactogen Ovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen 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 Placental Lactogen 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-Gln-His-Pro-Pro.
Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.85 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).

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:

Cytokeratin 5 Human Recombinant

Keratin 5, KRT5, EBS2, Epidermolysis Bullosa Simplex 2 Dowling-Meara/Kobner/Weber-Cockayne Types, Keratin 5 (Epidermolysis Bullosa Simplex,Dowling-Meara/Kobner/Weber-Cockayne Types), 58 KDa Cytokeratin, Type-II Keratin Kb5, CK-5, K5, DDD1, CK5, DDD, KRT5A, cytokeratin-5, Keratin, Type II Cytoskeletal 5, Cytokeratin-5, Keratin-5.

Product # :

PRO-1940

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Description

KRT5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 613 amino acids (1-590) and having a molecular mass of 64.8 kDa.KRT5 is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The KRT5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Cytokeratin 5 (KRT5) belongs to the keratin gene family. The type II cytokeratins are comprised of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed throughout differentiation of simple and stratified epithelial tissues. The type II cytokeratins are clustered in a region of chromosome 12q12-q13. The KRT5 type II cytokeratin is specifically expressed in the basal layer of the epidermis with family member KRT14. Mutations in these genes are linked with a complex of diseases termed epidermolysis bullosa simplex.
Synonyms
Keratin 5, KRT5, EBS2, Epidermolysis Bullosa Simplex 2 Dowling-Meara/Kobner/Weber-Cockayne Types, Keratin 5 (Epidermolysis Bullosa Simplex,Dowling-Meara/Kobner/Weber-Cockayne Types), 58 KDa Cytokeratin, Type-II Keratin Kb5, CK-5, K5, DDD1, CK5, DDD, KRT5A, cytokeratin-5, Keratin, Type II Cytoskeletal 5, Cytokeratin-5, Keratin-5.
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 MGSMSRQSSV SFRSGGSRSF STASAITPSV SRTSFTSVSR SGGGGGGGFG RVSLAGACGV GGYGSRSLYN LGGSKRISIS TSGGSFRNRF GAGAGGGYGF GGGAGSGFGF GGGAGGGFGL GGGAGFGGGF GGPGFPVCPP GGIQEVTVNQ SLLTPLNLQI DPSIQRVRTE EREQIKTLNN KFASFIDKVR FLEQQNKVLD TKWTLLQEQG TKTVRQNLEP LFEQYINNLR RQLDSIVGER GRLDSELRNM QDLVEDFKNK YEDEINKRTT AENEFVMLKK DVDAAYMNKV ELEAKVDALM DEINFMKMFF DAELSQMQTH VSDTSVVLSM DNNRNLDLDS IIAEVKAQYE EIANRSRTEA ESWYQTKYEE LQQTAGRHGD DLRNTKHEIS EMNRMIQRLR AEIDNVKKQC ANLQNAIADA EQRGELALKD ARNKLAELEE ALQKAKQDMA RLLREYQELM NTKLALDVEI ATYRKLLEGE ECRLSGEGVG PVNISVVTSS VSSGYGSGSG YGGGLGGGLG GGLGGGLAGG GSGSYYSSSS GGVGLSGGLS VGGSGFSASS GRGLGVGFGS GGGSSSSVKF VSTTSSSRKS FKS.

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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