Search: 1000 results found for "Septin"

Description:

Leptin Human Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-228

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Description

Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile water or 0.4% NaHCO3 pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 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:

Leptin Antagonist Triple Mutant Mouse Recombinant

Product # :

CYT-354

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Description

Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, LEP was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

ProSpec’s Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting Leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.201 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. 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:

Leptin Rat Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-227

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Shipped at Room temp

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Description

Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

Biological activity of Leptin Rat is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-His.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.201 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).2. Analysis by RP-HPLC, using a calibrated solution of Leptin rat as a Reference Standard.

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

Description:

Leptin Antagonist Triple Mutant Pegylated Mouse Recombinant

Product # :

CYT-566

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Description

Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Mouse Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

Leptin Antagonist Triple Mutant Mouse Recombinant half-life in circulation after SC injection was over 20 hours.
Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Mouse Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.

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Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. 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:

L-Selectin Human Recombinant, Sf9

Selectin L, Leukocyte-Endothelial Cell Adhesion Molecule 1, CD62 Antigen-Like Family Member L, Leukocyte Surface Antigen Leu-8, Lymphocyte Adhesion Molecule 1, Lymph Node Homing Receptor, Gp90-MEL, LECAM1, LYAM1, LNHR, TQ1, Leukocyte Adhesion Molecule, Pln Homing Receptor, CD62L Antigen, L-Selectin, CD62L, PLNHR, LAM-1, LAM1, LEU8, LSEL, L-selectin.

Product # :

PRO-2487

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Description

L-Selectin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 303 amino acids (52-345a.a.) and having a molecular mass of 34.1kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).L-Selectin is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
L-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. The L-Selectin molecule is composed of various domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.
L-selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin may be shed by proteolytic cleavage and circulating levels in biological fluids may be used as an indicator of various pathological conditions. L-Selectin is cleaved by ADAM17.
L-selectin works as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will attach to leukocytes expressing L-selectin, which causes the leukocytes to become localized at that juncture. The receptor is also located on the cell surfaces of "naive" T cells, which have not yet encountered their particular antigen. This surface expression is lost following the cells activation.
Synonyms
Selectin L, Leukocyte-Endothelial Cell Adhesion Molecule 1, CD62 Antigen-Like Family Member L, Leukocyte Surface Antigen Leu-8, Lymphocyte Adhesion Molecule 1, Lymph Node Homing Receptor, Gp90-MEL, LECAM1, LYAM1, LNHR, TQ1, Leukocyte Adhesion Molecule, Pln Homing Receptor, CD62L Antigen, L-Selectin, CD62L, PLNHR, LAM-1, LAM1, LEU8, LSEL, L-selectin.
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
ADPWTYHYSE KPMNWQRARR FCRDNYTDLV AIQNKAEIEY LEKTLPFSRS YYWIGIRKIG GIWTWVGTNK SLTEEAENWG DGEPNNKKNK EDCVEIYIKR NKDAGKWNDD ACHKLKAALC YTASCQPWSC SGHGECVEII NNYTCNCDVG YYGPQCQFVI QCEPLEAPEL GTMDCTHPLG NFSFSSQCAF SCSEGTNLTG IEETTCGPFG NWSSPEPTCQ VIQCEPLSAP DLGIMNCSHP LASFSFTSAC TFICSEGTEL IGKKKTICES SGIWSNPSPI CQKLDKSFSM IKEGDYNHHH HHH.

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:

Vasoactive Intestinal Peptide

Product # :

HOR-043

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Description

Vasoactive Intestinal Peptide Synthetic is a single, non-glycosylated polypeptide chain containing 28 amino acids, having a molecular mass of 3325 Dalton and a Molecular formula of C147H238N44O42S .

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Vasoactive Intestinal Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Vasoactive Intestinal Peptide 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 Vasoactive Intestinal Peptide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-Met-Ala-Val-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn-NH2.
Background
Vasoactive Intestinal Peptide (VIP), a prominent member of the glucagon-secretin peptide superfamily, plays a multifaceted role as a neuropeptide and neurotransmitter. This research paper aims to provide an extensive analysis of VIP, exploring its biochemical properties, diverse physiological functions, and potential therapeutic applications in various disease conditions.
Vasoactive Intestinal Peptide (VIP), originally identified for its potent vasodilatory properties in the gastrointestinal system, has since been recognized for its wide-ranging physiological effects throughout the body. As a neuropeptide and neurotransmitter.
VIP, a 28-amino acid peptide, exhibits a diverse range of biological activities due to its interactions with multiple G protein-coupled receptors (GPCRs) from the VIP/PACAP receptor family (Harmar et al., 2012). These receptors are expressed in various tissues and cells, enabling VIP to exert its pleiotropic effects.
VIP is involved in the regulation of numerous physiological processes. It functions as a potent vasodilator, modulates smooth muscle activity in the gastrointestinal tract, and participates in neurotransmission in the central and peripheral nervous systems (Lelievre et al., 2008). Additionally, VIP has immunomodulatory properties, influencing immune cell functions and inflammatory responses (Delgado et al., 2004).
VIP serves as a neurotransmitter in the central nervous system, where it contributes to various neuronal functions, including learning, memory, and sensory perception (Deng et al., 2015). Moreover, VIP has demonstrated neuroprotective effects in neurodegenerative disorders, making it a potential therapeutic target for neuroprotection and neuroregeneration (Delgado et al., 2002).
VIP's diverse physiological functions offer potential therapeutic applications in various disease contexts. Research has explored its potential in the treatment of inflammatory diseases, neurodegenerative disorders, and gastrointestinal disorders (Delgado et al., 2013). Furthermore, VIP-based therapies are being investigated for their neuroprotective potential in brain injuries and stroke.
As the research on VIP continues to progress, further investigation is warranted to uncover the precise mechanisms of action and potential clinical applications in medicine. VIP stands as a remarkable example of a neuropeptide with extensive physiological roles and therapeutic potential in various disease conditions.
What is the molecular weight/Mw of VASOACTIVE INTESTINAL PEPTIDE Protein?
VASOACTIVE INTESTINAL PEPTIDE Protein has a total Mw of 3.32kDa.

What is the Purity of VASOACTIVE INTESTINAL PEPTIDE Protein?
VASOACTIVE INTESTINAL PEPTIDE Protein is >97% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of VASOACTIVE INTESTINAL PEPTIDE Protein?
H-His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-Gln-Met-Ala-Val-Lys-Lys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn-NH2.

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

What is the endotoxin level for VASOACTIVE INTESTINAL PEPTIDE Protein?
The endotoxin level is minimal, VASOACTIVE INTESTINAL PEPTIDE 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:

Follistatin Human Recombinant, Sf9

Follistatin, FS, Activin-Binding Protein, Follistatin Isoform FST317, FST.

Product # :

CYT-865

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Description

FST produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 295 amino acids (30-317a.a.) and having a molecular mass of 32.5kDa.FST is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

FST protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
Synonyms
Follistatin, FS, Activin-Binding Protein, Follistatin Isoform FST317, FST.
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
MGNCWLRQAK NGRCQVLYKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DFKVGRGRCS LCDELCPDSK SDEPVCASDN ATYASECAMK EAACSSGVLL EVKHSGSCNH HHHHH
Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN, SF9 Protein?
FOLLISTATIN HUMAN, SF9 Protein has a total Mw of 32.5kDa.

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

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

What is the amino acid sequence of FOLLISTATIN HUMAN, SF9 Protein?
MGNCWLRQAK NGRCQVLYKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DFKVGRGRCS LCDELCPDSK SDEPVCASDN ATYASECAMK EAACSSGVLL EVKHSGSCNH HHHHH.

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

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

Selenocysteinyl-tRNA(Sec) synthase Mouse Recombinant

AA986712, D5Ertd135e, SecS, SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein, SepSecS.

Product # :

ENZ-1081

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Description

SEPSECS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 527 amino acids (1-504 a.a.) and having a molecular mass of 57.7kDa.SEPSECS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SEPSECS protein solution (0.25 mg/ml) is formulated in 20mM Tris-HCl buffer (pH7.5) 1mM DTT, 0.2M NaCl and 50% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
SEPSECS catalyzes the last step of sec synthesis by converting O-phosphoseryl-tRNA(sec) to selenocysteinyl-tRNA(sec) using selenophosphate as the selenium donor. Furthermore, SEPSECS protein is considered a specific marker of autoimmune hepatitis.
Synonyms
AA986712, D5Ertd135e, SecS, SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein, SepSecS.
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 MGSMNPESFA AGERRVSPAY VRQGCEARRA HEHLIRLLLE QGKCPEDGWD ESTLELFLHE LAVMDSNNFL GNCGVGEREG RVASALVARR HYRFIHGIGR SGDISAVQPK AAGSSLLNKI TNSLVLNVIK LAGVHSVASC FVVPMATGMS LTLCFLTLRH
KRPKAKYIIW PRIDQKSCFK SMVTAGFEPV VIENVLEGDE LRTDLKAVEA KIQELGPEHI LCLHSTTACF APRVPDRLEE LAVICANYDI PHVVNNAYGL QSSKCMHLIQ QGARVGRIDA FVQSLDKNFM VPVGGAIIAG FNEPFIQDIS KMYPGRASAS PSLDVLITLL SLGCSGYRKL
LKERKEMFVY LSTQLKKLAE AHNERLLQTP HNPISLAMTL KTIDGHHDKA VTQLGSMLFT RQVSGARAVP LGNVQTVSGH TFRGFMSHAD NYPCAYLNAA AAIGMKMQDV DLFIKRLDKC LNIVRKEQTR ASVVSGADRN KAEDADIEEM ALKLDDVLGD VGQGPAL.

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

Description:

Leptin Salamander Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.

Product # :

CYT-704

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Leptin Salamander Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of 16kDa. The Salamander Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 99.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.

Biological Activity

By inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity in that test is similar to that of mouse leptin.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized recombinant salamander leptin although stable at room temperature for several weeks, should be stored desiccated below -18C. Upon reconstitution of recombinant salamander leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization recombinant salamander leptin can be stored at +4C for at least two weeks.
Solubility
It is recommended to reconstitute the lyophilized Salamander Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the ten N-terminal amino acids was determined and was found to be Ala-Ile-Met-Val-Asp-Gln-Leu-Arg-Met-Asp.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.104 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:

Neurotensin Human Recombinant, sf9

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

Product # :

PRO-2374

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Description

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

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

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

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

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

Description:

Leptin Mutant D23L Human Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-1243

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Quantity :

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source
formulation
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biological activity
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Description

Human Leptin Mutant D23L is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. Leptin Mutant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

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

Purity

Greater than 95.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

Human Leptin Mutant D23L is fully biologically active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Human Leptin Mutant D23L although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Mutant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids of recombinant human leptin was determined and was found to be Ala-Val-Pro-Ile-Gln.
Background
Leptin’s main part is to regulate long-term energy balance. Leptin is a hormone which mainly produced by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

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:

Semaphorin 3C Human Recombinant

Semaphorin 3C ,Semaphorin-3C, Semaphorin-3C isoform2, SEMA3C, Semaphorin-E, SEMAE, Sema E, SemE, SEME, Semaphorin E

Product # :

PRO-2750

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Quantity :

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source
formulation
purity
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Description

SEMA3C Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (21-738 a.a) containing a total of 951 amino acids, having a molecular mass of 107.2kDa. SEMA3C is fused to a 233 amino acid hIgG-Tag at C-terminus,and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The SEMA3C solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
SEMA3C, also known as Semaphorin 3C, is a member of the semaphorin family 3 that are grouped into 8 major classes based on phylogenetic tree analyses and structure. Class 3 have an important function after traumatic central nervous system injuries. SEMA3C regulates neuronal and non-neuronal cells associated with the traumatic injury due to their presence in the scar tissue. SEMA3C is expressed in all somatic motor neurons, in cardiac neural crest cells during development and in lung buds. The SEMA3C functions are mediated through binding to the Plexin-D1 and Neuropilin 1 or Neuropilin 2 coreceptor complex. SEMA3C activates integrins in certain cells, so besides its repulsive activities, it also acts as a chemoattractant.
Synonyms
Semaphorin 3C ,Semaphorin-3C, Semaphorin-3C isoform2, SEMA3C, Semaphorin-E, SEMAE, Sema E, SemE, SEME, Semaphorin E
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
GSSQPQARVY LTFDELRETK TSEYFSLSHH PLDYRILLMD EDQDRIYVGS KDHILSLNIN NISQEALSVF WPASTIKVEE CKMAGKDPTH GCGNFVRVIQ TFNRTHLYVC GSGAFSPVCT YLNRGRRSED QVFMIDSKCE SGKGRCSFNP NVNTVSVMIN EELFSGMYID FMGTDAAIFR SLTKRNAVRT DQHNSKWLSE PMFVDAHVIP DGTDPNDAKV YFFFKEKLTD NNRSTKQIHS MIARICPNDT GGLRSLVNKW TTFLKARLVC SVTDEDGPET HFDELEDVFL LETDNPRTTL VYGIFTTSSS VFKGSAVCVY HLSDIQTVFN GPFAHKEGPN HQLISYQGRI PYPRPGTCPG GAFTPNMRTT KEFPDDVVTF IRNHPLMYNS IYPIHKRPLI VRIGTDYKYT KIAVDRVNAA DGRYHVLFLG TDRGTVQKVV VLPTNNSVSG ELILEELEVF KNHAPITTMK ISSKKQQLYV SSNEGVSQVS LHRCHIYGTA CADCCLARDP YCAWDGHSCS RFYPTGKRRS AAQDVRHGNP LTQCRGFNLK AYRNAAEIVQ YGVKNNTTFL ECAPKSPQAS IKWLLQKDKD AAKEVKLNER IIATSQGLLI RSVQGSDQGL YHCIATENSF KQTIAKINFK VLDSEMVAVV TDKWSPWTWA SSVRALPFHP KDIMGAFSHS EMQMINQYCK DTRQQHQQGD ESQKMRGDYG KLKALINSLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG K

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

Description:

Leptin Quadruple Antagonist Mouse Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-1257

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Leptin Quadruple Antagonist Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino, an additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. The Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. Leptin Quadruple Antagonist Mouse Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

The Mouse Leptin Quadruple anatagonist was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

Purity

Greater than 98.0% as determined by:

(a) Gel filtration analysis.

(b) Analysis by SDS-PAGE.

Biological Activity

Leptin Quadruple Antagonist Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Mouse Leptin Quadruple Antagonist also inhibits various leptin effects in several in vitro bioassays. The inhibitory activity of Mouse Leptin Quadruple Antagonist was increased 14 to 60 fold as measured by various criteria such as binding properties to human leptin binding domain and in vitro and in vivo bioassays as compared to mouse leptin antagonist.

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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Antagonist Quadruple Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization LEP Antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids of mouse super-active leptin antagonist was determined and was found to be Ala-Val-Pro-Ile-Gln.
Background
Leptin is produced by adipocytes and its main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene and effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. 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:

Leptin Mouse Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-351

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Leptin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16 kDa. The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The mouse Leptin was lyophilized from a concentrated (1mg/ml) solution containing 0.0045mM NaHCO3.

Purity

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

Biological Activity

Biological activity of Mouse Leptin is performed by including proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVPIQKVQDD TKTLIKTIVT RINDISHTQS VSAKQRVTGL DFIPGLHPIL SLSKMDQTLA VYQQVLTSLP SQNVLQIAND LENLRDLLHL LAFSKSCSLP QTSGLQKPES LDGVLEASLY STEVVALSRL QGSLQDILQQ LDVSPEC.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.20 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH-8.0. 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:

Thymopentin

Product # :

HOR-241

Price :

Quantity :

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formulation
purity
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Description

Thymopentin has a molecular formula of C30H49N9O9, Arg-Lys-Asp-Val-Tyr-OH having an Mw of 679.8 Dalton.

Formulation

The protein (1mg/ml) was lyophilized with no additives.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

What is the molecular weight/Mw of THYMOPENTIN Protein? THYMOPENTIN Protein has a total Mw of 0.67kDa. What is the Purity of THYMOPENTIN Protein? THYMOPENTIN Protein is >99% pure as determined by SDS-PAGE. What is the Biological Activity of THYMOPENTIN Protein? The biological functionality of THYMOPENTIN Protein will be determined in the future. What applications can THYMOPENTIN Protein be used in? THYMOPENTIN Protein can probably be used in western blot, ELISA and Lateral Flow. What is the endotoxin level for THYMOPENTIN Protein? The endotoxin level is minimal, THYMOPENTIN Protein was purified using conventional chromatography techniques.

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Introduction
Thymopentin, also known as TP-5, is a synthetic pentapeptide which is the active site of the naturally occurring hormone thymopoietin with immunomodulating properties (corresponding to the amino acids 32-36 of thymopoietin). Thymopentin enhances the production of thymic T cells and may help restore immunocompetence in immunosuppressed subjects. This agent also augments the effects of ionizing radiation by arresting cancer cells in the G2/M phase of the cell cycle.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymopentin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TP-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 Thymopentin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Holo Transferrin Human

Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

Product # :

PRO-315

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
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Description

Human Holo Transferrin is a glycoprotein of approximately 77 kDa.

Source

Human serum.

Formulation

The protein (10mg/ml) was lyophilized from 20mM NH4HC03 solution.
May contain traces of buffer salts.

Purity

Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.

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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
Physical Appearance
Sterile Filtered Pink lyophilized (freeze-dried) powder.
Stability
Store the lyophilized Holo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Holo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Human Virus Test
FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, HBc, HBV, HAV, HIV and Syphilis.
Iron Content
The Iron content was estimated by ICP and was found to be 1232 ppm.

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:

SEMAX

Product # :

HOR-033

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
purity
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Description

SEMAX Synthetic is a single, non-glycosylated polypeptide chain containing 7 amino acids, having a molecular mass of 813.92 Dalton and a Molecular formula of C37H51N19O1S.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SEMAX although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SEMAX 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 SEMAX in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-Met-Glu-His-Phe-Pro-Gly-Pro-OH.
Background
Semax, also known as ACTH(4-10) Pro-Gly-Pro, is a synthetic peptide that has been the subject of extensive research due to its potential neuroprotective and nootropic effects. This heptapeptide, derived from the adrenocorticotropic hormone (ACTH), has been shown to possess a wide range of biological activities, including enhancing memory, learning, and neurogenesis.
Semax is unique in its ability to cross the blood-brain barrier and exert its effects directly on the central nervous system. It has been shown to stimulate the release of brain-derived neurotrophic factor (BDNF), a protein that plays a crucial role in the survival of neurons and the growth of new neurons and synapses. Studies by Dolotov et al. (2006) have demonstrated that Semax can enhance memory and learning in rats, suggesting potential applications in cognitive enhancement and the treatment of cognitive disorders.
In addition to its nootropic effects, Semax has been shown to possess neuroprotective properties. Research by Stavchansky et al. (2008) found that Semax could protect neurons from oxidative stress and apoptosis, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.
Given its nootropic and neuroprotective effects, Semax has been proposed as a potential therapeutic agent for a variety of conditions, including cognitive disorders, stroke, and optic nerve disease. For instance, a study by Myasoedov et al. (2010) found that Semax could improve outcomes in patients with ischemic stroke, indicating its potential as a therapeutic agent in stroke recovery.
While research on Semax is promising, it is important to note that most studies have been conducted in animals or in vitro. More research is needed to fully understand the potential effects and applications of Semax in humans. However, the existing body of research suggests that Semax could be a promising tool in the treatment of cognitive disorders and neurodegenerative diseases.

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:

Semenogelin I Human Recombinant

CT103, dJ172H20.2, SEMG, SGI, Semenogelin-1, Semenogelin I, SEMG1.

Product # :

PRO-1732

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
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Description

SEMG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 462 amino acids (24-462) and having a molecular mass of 52kDa. SEMG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SEMG1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.5M NaCl, 10% glycerol, 250mM Imidazole, 0.1mM PMSF and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
SEMG1 is the predominant protein in semen. The secreted protein takes part in the formation of a gel matrix which encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes SEMG1 into smaller peptides, with each possibly having a separate function. The proteolysis process breaks down the gel matrix and allows the spermatozoa to shift more freely. 2 transcript variants encoding different isoforms have been found for SEMG1.
Synonyms
CT103, dJ172H20.2, SEMG, SGI, Semenogelin-1, Semenogelin I, SEMG1.
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 MGSQKGGSKG RLPSEFSQFP HGQKGQHYSG QKGKQQTESK GSFSIQYTYH VDANDHDQSR KSQQYDLNAL HKTTKSQRHL GGSQQLLHNK QEGRDHDKSK GHFHRVVIHH KGGKAHRGTQ NPSQDQGNSP SGKGISSQYS NTEERLWVHG LSKEQTSVSG AQKGRKQGGS QSSYVLQTEE LVANKQQRET KNSHQNKGHY QNVVEVREEH SSKVQTSLCP AHQDKLQHGS KDIFSTQDEL LVYNKNQHQT KNLNQDQQHG RKANKISYQS SSTEERRLHY GENGVQKDVS QSSIYSQTEE KAQGKSQKQI TIPSQEQEHS QKANKISYQS SSTEERRLHY GENGVQKDVS QRSIYSQTEK LVAGKSQIQA PNPKQEPWHG ENAKGESGQS TNREQDLLSH EQKGRHQHGS HGGLDIVIIE QEDDSDRHLA QHLNNDRNPL FT.

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:

Selectin P Ligand Human Recombinant

Cutaneous Lymphocyte-Associated Associated Antigen, Selectin P Ligand, PSGL-1, CD162 Antigen, P-Selectin Glycoprotein Ligand 1, CLA.

Product # :

PRO-2714

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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description
source
formulation
purity
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Description

SELPLG Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 496 amino acids (42-295 a.a) and having a molecular mass of 53.4kDa.SELPLG is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The SELPLG solution (1mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
SELPLG glycoprotein functions as a high affinity counter-receptor for the cell adhesion selectin molecules (P, E and L) located in stimulated T lymphocytes and myeloid cells. SELPLG binds leukocytes to activated platelets or endothelia expressing selectins, a vital role in leukocyte trafficking throughout inflammation. In order to have a high-affinity binding activity SELPLG needs two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans. Polymorphisms and abnormal expression of SELPLG are linked to defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.
Synonyms
Cutaneous Lymphocyte-Associated Associated Antigen, Selectin P Ligand, PSGL-1, CD162 Antigen, P-Selectin Glycoprotein Ligand 1, CLA.
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
DGSQATEYEY LDYDFLPETE PPEMLRNSTD TTPLTGPGTP ESTTVEPAAR RSTGLDAGGA VTELTTELAN MGNLSTDSAA MEIQTTQPAA TEAQTTPLAA TEAQTTRLTA TEAQTTPLAA TEAQTTPPAA TEAQTTQPTG LEAQTTAPAA MEAQTTAPAA MEAQTTPPAA MEAQTTQTTA MEAQTTAPEA TEAQTTQPTA TEAQTTPLAA MEALSTEPSA TEALSMEPTT KRGLFIPFSV SSVTHKGIPM AASNLSVLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH

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

Description:

Semaglutide

Product # :

HOR-048

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
formulation
purity
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HPLC, MS

Description

Semaglutide Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 4113 Dalton and a Molecular formula of C187H291N45O59.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

HPLC, MS

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Semaglutide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Semaglutide 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 Semaglutide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-His-Aib-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Val-Ser-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-Lys(AEEAc-AEEAc-γ-Glu-17-carboxyheptadecanoyl)-Glu-Phe-Ile-Ala-Trp-Leu-Val-Arg-Gly-Arg-Gly-OH.
Background
Semaglutide, a glucagon-like peptide-1 receptor agonist (GLP-1 RA), has emerged as a breakthrough in the field of diabetes management and metabolic disorders. It is recognized for its potent glucose-lowering effects, weight management properties, and cardiovascular benefits. Beyond diabetes, semaglutide is under investigation for its potential applications in obesity treatment and other related conditions. This research aims to comprehensively explore semaglutide, shedding light on its multifaceted mechanisms of action and its broader therapeutic implications.
The primary objective of this research is to elucidate the mechanisms underlying the glucose-lowering and metabolic effects of semaglutide. In vitro and in vivo experiments will be conducted to investigate how semaglutide interacts with GLP-1 receptors, influences insulin secretion, and modulates glucose homeostasis. Understanding these mechanisms is crucial for harnessing the full therapeutic potential of semaglutide.
The second objective is to assess the clinical relevance of semaglutide in diabetes management. Clinical trials involving individuals with type 2 diabetes will be conducted to evaluate the efficacy, safety, and long-term outcomes of semaglutide treatment. These investigations may provide valuable insights into its use as a monotherapy or adjunct therapy in diabetes care.
The third objective is to explore the potential applications of semaglutide beyond diabetes. Research will investigate its role in obesity treatment, cardiovascular risk reduction, and non-alcoholic fatty liver disease (NAFLD) management. Understanding the multifaceted properties of semaglutide may open new avenues for therapeutic interventions in various metabolic and cardiovascular conditions.
By delving into the diverse functions of semaglutide, this research aims to expand our understanding of its therapeutic potential and clinical applications. The findings may contribute to improved treatment strategies for individuals affected by diabetes, obesity, and related metabolic disorders.

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:

Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant, Sf9

Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.

Product # :

PRO-2219

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Description

SPINT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 176 amino acids (28-197 a.a.) and having a molecular mass of 20kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SPINT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SPINT2 protein solution (0.2mg/ml) contains phosphate buffered saline (pH 7.4) and 10% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
SPINT2 is a transmembrane protein acts as an inhibitor of HGF activator. SPINT2 inhibits plasmin, plasma and tissue kallikrein, and factor XIa. SPINT2 has two extracellular Kunitz domains that inhibit few serine proteases. SPINT2 is assumed tumor suppressor, mutations in SPINT2 leads to a congenital sodium diarrhea.
Synonyms
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 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
ADRERSIHDF CLVSKVVGRC RASMPRWWYN VTDGSCQLFV YGGCDGNSNN YLTKEECLKK CATVTENATG DLATSRNAAD SSVPSAPRRQ DSEDHSSDMF NYEEYCTANA VTGPCRASFP RWYFDVERNS CNNFIYGGCR GNKNSYRSEE ACMLRCFRQQ ENPPLPLGSK HHHHHH.

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

Description:

Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant, Sf9

Serpin Family G Member 1, Serpin Peptidase Inhibitor, Clade G (C1 Inhibitor), Member 1, Plasma Protease C1 Inhibitor, C1 Esterase Inhibitor, C1-Inhibiting Factor, Serpin G1, C1NH, C1IN, Serine (Or Cysteine) Proteinase Inhibitor, Clade G (C1 Inhibitor), Member 1, (Angioedema, Hereditary), Serine/Cysteine Proteinase Inhibitor Clade G Member 1, Serpin Peptidase Inhibitor Clade G Member 1, Complement Component 1 Inhibitor, Angioedema, Hereditary, C1 Inh, C1INH, C1Inh, HAE1, HAE2.

Product # :

PRO-2589

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Description

SERPING1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 489 amino acids (23-500a.a.) and having a molecular mass of 54.2kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).SERPING1 is expressed with an 11 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SERPING1 protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 takes part in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. Lack of SERPING1 results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.
Synonyms
Serpin Family G Member 1, Serpin Peptidase Inhibitor, Clade G (C1 Inhibitor), Member 1, Plasma Protease C1 Inhibitor, C1 Esterase Inhibitor, C1-Inhibiting Factor, Serpin G1, C1NH, C1IN, Serine (Or Cysteine) Proteinase Inhibitor, Clade G (C1 Inhibitor), Member 1, (Angioedema, Hereditary), Serine/Cysteine Proteinase Inhibitor Clade G Member 1, Serpin Peptidase Inhibitor Clade G Member 1, Complement Component 1 Inhibitor, Angioedema, Hereditary, C1 Inh, C1INH, C1Inh, HAE1, HAE2.
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
ADPEFNPNAT SSSSQDPESL QDRGEGKVAT TVISKMLFVE PILEVSSLPT TNSTTNSATK ITANTTDEPT TQPTTEPTTQ PTIQPTQPTT QLPTDSPTQP TTGSFCPGPV TLCSDLESHS TEAVLGDALV DFSLKLYHAF SAMKKVETNM AFSPFSIASL LTQVLLGAGE NTKTNLESIL SYPKDFTCVH QALKGFTTKG VTSVSQIFHS PDLAIRDTFV NASRTLYSSS PRVLSNNSDA NLELINTWVA KNTNNKISRL LDSLPSDTRL VLLNAIYLSA KWKTTFDPKK TRMEPFHFKN SVIKVPMMNS KKYPVAHFID QTLKAKVGQL QLSHNLSLVI LVPQNLKHRL EDMEQALSPS VFKAIMEKLE MSKFQPTLLT LPRIKVTTSQ DMLSIMEKLE FFDFSYDLNL CGLTEDPDLQ
VSAMQHQTVL ELTETGVEAA AASAISVART LLVFEVQQPF LFVLWDQQHK FPVFMGRVYD PRAHHHHHH.

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:

Serine Peptidase Inhibitor Kazal Type 7 Human Recombinant

Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.

Product # :

PRO-1507

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Description

SPINK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 89 amino acids (20-85) and having a molecular mass of 9.6 kDa.SPINK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SPINK7 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Serine peptidase inhibitor Kazal type 7 (SPINK7) which includes one Kazal-like domain is most likely serine protease inhibitor. Diseases linked with SPINK7 include esophageal cancer, and oral squamous cell carcinoma
Synonyms
Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.
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 MGSSEAASLS PKKVDCSIYK KYPVVAIPCP ITYLPVCGSD YITYGNECHL CTESLKSNGR VQFLHDGSC.

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:

Relaxin-2 Human Recombinant, Sf9

Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.

Product # :

PRO-2406

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Description

RLN2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 170 amino acids (25-185a.a.) and having a molecular mass of 19.3kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).RLN2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

RLN2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Prorelaxin H2 (RLN2) is a member of the insulin gene superfamily. This family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing oxytocin and vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.
Synonyms
Relaxin 2, Relaxin, Ovarian, Of Pregnancy, Prorelaxin H2, Relaxin H2, H2-Preprorelaxin, Relaxin 2 (H2), BA12D24.1.1, BA12D24.1.2, H2-RLX, RLXH2, H2.
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
ADPDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFCHHHHHH.

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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