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Description:

LL-37

LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.

Product # :

HOR-041

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Description

LL-37 Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 4493 Dalton and a Molecular formula of C205H340N60O53.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Synonyms
LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized LL-37 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LL-37 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 LL-37 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-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH.
Background
LL-37, a prominent member of the human cathelicidin family, has emerged as a pivotal host defense peptide with diverse biological functions. This research paper aims to provide a comprehensive analysis of LL-37, elucidating its biochemical properties, antimicrobial activity, immunomodulatory effects, and potential therapeutic applications.
LL-37, derived from the precursor protein hCAP18, plays a crucial role in innate immunity and host defense against microbial pathogens. Beyond its well-established antimicrobial properties, LL-37 exhibits various immunomodulatory effects, making it an intriguing target for therapeutic interventions (Lai & Gallo, 2009). This paper aims to delve into the complexities of LL-37, uncovering its multifaceted nature and potential clinical applications.
LL-37 is a cationic peptide characterized by a helical structure that facilitates its interaction with microbial membranes. Its amphipathic nature enables it to penetrate microbial membranes, leading to disruption and subsequent cell death (Zaiou, 2007). Additionally, LL-37 can undergo proteolytic processing to release smaller bioactive fragments with distinct functions (Bowdish et al., 2005).
LL-37's antimicrobial activity extends beyond direct microbial killing. It also exhibits immunomodulatory effects, stimulating the recruitment of immune cells and promoting the clearance of pathogens through phagocytosis (Scott et al., 2002). Furthermore, LL-37 can neutralize endotoxins, reducing inflammation caused by microbial products (Davidson et al., 2004).
LL-37 possesses immunomodulatory properties that influence various immune cells, including neutrophils, macrophages, dendritic cells, and lymphocytes (Nagaoka et al., 2001). It can promote the differentiation and maturation of immune cells, modulate cytokine production, and contribute to wound healing and tissue repair (van Harten et al., 2018).
The multifunctional nature of LL-37 renders it a promising candidate for various therapeutic applications. LL-37-based therapies are being explored in wound healing, infectious diseases, and immune-related disorders (Pena et al., 2014). Furthermore, LL-37 has shown potential as a vaccine adjuvant, enhancing the immune response to antigens (Howell et al., 2018).
LL-37's diverse roles in immunity and host defense warrant further research to unravel its precise mechanisms of action and potential applications in clinical medicine. As we deepen our understanding of LL-37's complexities, its therapeutic potential continues to expand, offering exciting prospects for the future.

What is the molecular weight/Mw of LL-37 Protein?
LL-37 Protein has a total Mw of 4.493kDa.

What is the Purity of LL-37 Protein?
LL-37 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of LL-37 Protein?
The biological functionality of LL-37 Protein will be determined in the future.

What is the amino acid sequence of LL-37 Protein?
H-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH.

What applications can LL-37 Protein be used in?
LL-37 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LL-37 Protein?
The endotoxin level is minimal, LL-37 Protein was purified using conventional chromatography techniques.

Who supplies LL-37 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of LL-37?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Oxyntomodulin Porcine Recombinant

Product # :

HOR-292

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Description

Oxyntomodulin Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 37 amino acids and having a molecular mass of 4420.86 Dalton. The OXM is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

More Info

Introduction
OXM a 37 amino acid peptide which contains the glucagon sequence extended by a C-terminal basic octapeptide, its primary structure is identical in all mammals except in pig and cattle. OXM is released from the gut during digestion, together with glicentin another octapeptide containing molecule. It is considered as a putative physiological regulator of gastric acid secretion, it inhibits histamine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Oxyntomodulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OXM 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 Oxyntomodulin in 20mM acetic acid.
Amino Acid Sequence
His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-Lys-Arg-Asn-Lys-Asn-Asn-Ile-Ala.
Background
What is the molecular weight/Mw of OXYNTOMODULIN Protein?
OXYNTOMODULIN Protein has a total Mw of 4.420kDa.

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

What is the Purity of OXYNTOMODULIN Protein?
OXYNTOMODULIN Protein is >99% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of OXYNTOMODULIN Protein?
His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-Lys-Arg-Asn-Lys-Asn-Asn-Ile-Ala.

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

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

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

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

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

Description:

Thyrostimulin Beta Human Recombinant

Glycoprotein hormone beta-5, ZLUT1, GPHB5, GPB5.

Product # :

HOR-257

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Description

GPHB5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a total molecular mass of 13.34 kDa. The Thyrostimulin contains His tag which consists of 14 additional amino acids.The amino acid sequence of the recombinant human Thyrostimulin beta subunit is 100% homologous to the amino acid sequence of the human Thyrostimulin beta subunit without signal sequence. (N-terminal 24AA).Thyrostimulin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GPHB5 filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M Acetate buffer pH 4.

Purity

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

More Info

Introduction
Human thyrostimulin ranks among the glycoprotein hormone family. These hormones consist of two subunits, the common alpha- and specific beta-subunits, which associate noncovalently to form a heterodimer. The alpha-subunit combines with four distinct beta-subunits giving rise to four biologically active hormones in human: FSH, LH, TSH, and CG. FSH, LH, and TSH, mainly expressed in the anterior pituitary, are essential for coordinated endocrine regulation in the hypothalamus- pituitary axis and show to activate specific G protein–coupled receptors in the thyroid (TSH receptor) and gonads (LH and FSH receptors), respectively.
The heterodimeric glycoprotein hormones have only been identified in vertebrates and are highly conserved in organisms from primitive rayfin fish (Chondrostei) to human in both primary sequences and functional characteristics.
Corticotroph-derived glycoprotein hormone (CGH), also referred to as thyrostimulin, is a noncovalent heterodimer of glycoprotein hormone alpha 2 (GPHA2) and glycoprotein hormone beta 5 (GPHB5).
Recombinant A2/B5 heterodimeric glycoproteins activates human TSH receptors, but not LH and FSH receptors, and shows high affinity to TSH receptors in a radioligand receptor assay. The heterodimer also stimulates cAMP production and thymidine incorporation by cultured thyroid cells and increases serum thyroxine levels in TSH-suppressed rats in vivo. This new heterodimeric glycoprotein hormone was named as thyrostimulin based on its thyroid-stimulating activity. The expression of thyrostimulin in the anterior pituitary known to express TSH receptors suggested a paracrine mechanism.
Synonyms
Glycoprotein hormone beta-5, ZLUT1, GPHB5, GPB5.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thyrostimulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GPHB5 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of ~ 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this protein is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MRGSHHHHHH GMASASSGNL RTFVGCAVRE FTFLAKKPGC RGLRITTDAC WGRCETWEKP ILEPPYIEAH HRVCTYNETK QVTVKLPNCA PGVDPFYTYP VAIRCDCGAC STATTECETI.
Background
What is the molecular weight/Mw of GPHB5 Protein?
GPHB5 Protein has a total Mw of 13.34kDa.

What is the source or expression system of GPHB5 Protein?
Escherichia Coli.

What is the Purity of GPHB5 Protein?
GPHB5 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GPHB5 Protein?
The biological functionality of GPHB5 Protein will be determined in the future.

What is the amino acid sequence of GPHB5 Protein?
MRGSHHHHHH GMASASSGNL RTFVGCAVRE FTFLAKKPGC RGLRITTDAC WGRCETWEKP ILEPPYIEAH HRVCTYNETK QVTVKLPNCA PGVDPFYTYP VAIRCDCGAC STATTECETI.

What applications can GPHB5 Protein be used in?
GPHB5 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GPHB5 Protein?
The endotoxin level is minimal, GPHB5 Protein was purified using conventional chromatography techniques.

Who supplies recombinant GPHB5 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of GPHB5?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Insulin (20-110 a.a) Human Recombinant

Product # :

CYT-1237

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Description

The Insulin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Insulin His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 91 amino acid residues of the Insulin Human, 20-110 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Insulin 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
Background
Insulin participates in the metabolism of carbohydrates, proteins and fats by regulating glucose homeostasis in the body. Insulin decreases blood glucose concentration. Insulin hormone facilitates the uptake of glucose into cells, mainly in muscle and fat tissues, and stimulates the liver to store glucose as glycogen. Insulin also inhibits the production of gluconeogenesis and promotes the synthesis of proteins and lipids. Insulin increases cell permeability to monosaccharides, fatty acids and amino acids. Insulin accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis in liver.

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:

Urocortin 3 Human Recombinant

Stresscopin, urocortin-iii.

Product # :

HOR-056

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Description

The UCN3Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The UCN3His-Tagged Fusion Protein, produced in E. coli, is a 20kDa protein containing 161 amino acid residues of the UCN3Human, 1-161 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Synonyms
Stresscopin, urocortin-iii.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized UCN3at -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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
Urocortin 3 also known as UCN3 is a part of the corticotropin-releasing factor (CRF) family of peptides, which are involved in metabolism, stress response and neuroendocrine regulation. UCN3 exerts its biological effects through interactions with CRFR2. UCN3 takes a main part in mediating few important biological processes, specially those associated with energy metabolism, stress response and the regulation of the hypothalamic-pituitary-adrenal (HPA) axis. UCN3 expressed mainly in the brain in areas such as the hypothalamus, as well as in peripheral tissues, including the heart and adipose tissue.
What is the molecular weight/Mw of UCN3 HUMAN Protein?
UCN3 HUMAN Protein has a total Mw of 20kDa.

What is the source or expression system of UCN3 HUMAN Protein?
Escherichia Coli.

What is the Purity of UCN3 HUMAN Protein?
UCN3 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of UCN3 HUMAN Protein?
The biological functionality of UCN3 HUMAN Protein will be determined in the future.

What applications can UCN3 HUMAN Protein be used in?
UCN3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for UCN3 HUMAN Protein?
The endotoxin level is minimal, UCN3 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:

Stanniocalcin-2 Human Recombinant

Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.

Product # :

HOR-296

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Description

Stanniocalcin-2 Human Recombinant produced in HEK 293 cell line is a single, glycosylated, polypeptide chain containing 289 amino acids and having a total molecular mass of 31.9kDa (calculated). The Stanniocalcin contains four extra residues which were used as a spacer and 8 residues form the C-Terminal Flag- tag.Stanniocalcin is purified by proprietary chromatographic techniques.The amino acid sequence of the recombinant human Stanniocalcin-2 is 100% homologous to the amino acid sequence AA 25-302 of the human mature Human Stanniocalcin-2.

Source

HEK 293 cell line (Human embryonic kidney).

Formulation

Filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris buffer, 20mM NaCl, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
STC2 is a homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The encoded protein has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. Its C-terminus contains a cluster of histidine residues which may interact with metal ions. The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Constitutive over expression of human stanniocalcin 2 in mice resulted in pre- and postnatal growth restriction, reduced bone and skeletal muscle growth, and organomegaly. Expression of this gene is induced by estrogen and altered in some breast cancers.
Synonyms
Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.
Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized STC-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Stanniocalcin 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
Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
TDATNPPEGP QDRSSQQKGR LSLQNTAEIQ HCLVNAGDVG CGVFECFENN SCEIRGLHGI CMTFLHNAGKFDAQGKSFIK DALKCKAHAL RHRFGCISRK CPAIREMVSQ LQRECYLKHD LCAAAQENTR VIVEMIHFKDLLLHEPYVDL VNLLLTCGEE VKEAITHSVQ VQCEQNWGSL CSILSFCTSA IQKPPTAPPE RQPQVDRTKLSRAHHGEAGH HLPEPSSRET GRGAKGERGS KSHPNAHARG RVGGLGAQGP SGSSEWEDEQ SEYSDIRRAAADYKDDDDK.
Background
What is the molecular weight/Mw of STANNIOCALCIN-2 HUMAN Protein?
STANNIOCALCIN-2 HUMAN Protein has a total Mw of 31.9kDa.

What is the source or expression system of STANNIOCALCIN-2 HUMAN Protein?
HEK 293 cell line (Human embryonic kidney).

What is the Purity of STANNIOCALCIN-2 HUMAN Protein?
STANNIOCALCIN-2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of STANNIOCALCIN-2 HUMAN Protein?
The biological functionality of STANNIOCALCIN-2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of STANNIOCALCIN-2 HUMAN Protein?
TDATNPPEGP QDRSSQQKGR LSLQNTAEIQ HCLVNAGDVG CGVFECFENN SCEIRGLHGI CMTFLHNAGKFDAQGKSFIK DALKCKAHAL RHRFGCISRK CPAIREMVSQ LQRECYLKHD LCAAAQENTR VIVEMIHFKDLLLHEPYVDL VNLLLTCGEE VKEAITHSVQ VQCEQNWGSL CSILSFCTSA IQKPPTAPPE RQPQVDRTKLSRAHHGEAGH HLPEPSSRET GRGAKGERGS KSHPNAHARG RVGGLGAQGP SGSSEWEDEQ SEYSDIRRAAADYKDDDDK.

What applications can STANNIOCALCIN-2 HUMAN Protein be used in?
STANNIOCALCIN-2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for STANNIOCALCIN-2 HUMAN Protein?
The endotoxin level is minimal, STANNIOCALCIN-2 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant STANNIOCALCIN-2 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of STANNIOCALCIN-2 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

DIHEXA

Product # :

HOR-034

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Description

DIHEXA Synthetic is a single, non-glycosylated polypeptide chain containing 3 amino acids, having a molecular mass of 504.28 Dalton and a Molecular formula of C27H44N4O5.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized DIHEXA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DIHEXA 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 DIHEXA in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Hexanoyl-Tyr-Ile-Ahx-NH2.
Background
Dihexa, also known as N-hexanoic-Tyr-Ile-(6) aminohexanoic amide, is a potent and orally active small peptide that has been the focus of significant research due to its potential neurogenic and neuroprotective effects. This compound, derived from angiotensin IV, has been shown to possess a wide range of biological activities, including enhancing cognitive function, promoting neurogenesis, and potentially mitigating the effects of neurodegenerative diseases.
Dihexa's primary mechanism of action involves its interaction with hepatocyte growth factor (HGF) and its receptor, c-Met. By mimicking the effects of HGF, Dihexa can stimulate the c-Met receptor, leading to a cascade of events that promote neurogenesis and synaptic plasticity. Studies by Benoist et al. (2014) have demonstrated that Dihexa can enhance cognitive function in rats, suggesting potential applications in cognitive enhancement and the treatment of cognitive disorders.
In addition to its neurogenic effects, Dihexa has been shown to possess neuroprotective properties. Research by Kawas et al. (2017) found that Dihexa could protect neurons from apoptosis, suggesting potential applications in the treatment of neurodegenerative diseases such as Alzheimer's and Parkinson's disease.
Given its neurogenic and neuroprotective effects, Dihexa has been proposed as a potential therapeutic agent for a variety of conditions, including cognitive disorders, neurodegenerative diseases, and stroke. For instance, a study by Harding et al. (2018) found that Dihexa could improve outcomes in animal models of stroke, indicating its potential as a therapeutic agent in stroke recovery.
While research on Dihexa 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 Dihexa in humans. However, the existing body of research suggests that Dihexa 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:

C-Peptide

Product # :

HOR-046

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Description

C-Peptide Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3020 Dalton and a Molecular formula of C129H211N35O48S .

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized C-Peptide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution C-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 C-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-Glu-Ala-Glu-Asp-Leu-Gln-Val-Gly-Gln-Val-Glu-Leu-Gly-Gly-Gly-Pro-Gly-Ala-Gly-Ser-Leu-Gln-Pro-Leu-Ala-Leu-Glu-Gly-Ser-Leu-Gln-OH.
Background
C-peptide, a small peptide derived from proinsulin, has garnered increasing attention in recent years for its multifaceted physiological functions and clinical significance, particularly in the context of diabetes mellitus. While initially considered a mere byproduct of insulin synthesis, research has revealed that C-peptide exerts unique biological effects, extending beyond glycemic control. This research endeavors to comprehensively investigate the roles of C-peptide, shedding light on its diverse functions and potential applications in diabetes management and other areas of healthcare.
The primary objective of this study is to unravel the mechanisms underlying the physiological actions of C-peptide. In vitro experiments using cellular and tissue models will be conducted to explore how C-peptide interacts with cellular receptors and signaling pathways. This includes investigations into its influence on insulin secretion, glucose uptake, and endothelial function. Understanding these mechanisms is essential for delineating the potential therapeutic applications of C-peptide.
The second objective is to assess the clinical relevance of C-peptide in diabetes management. Clinical trials involving individuals with type 1 and type 2 diabetes will be conducted to evaluate the effects of exogenous C-peptide administration on glycemic control, insulin sensitivity, and microvascular complications. These studies may provide valuable insights into the use of C-peptide as an adjunct therapy in diabetes treatment.
The third objective is to explore the broader implications of C-peptide in healthcare. Research will investigate the potential role of C-peptide in conditions beyond diabetes, such as its effects on cardiovascular health, neuroprotection, and wound healing. Understanding the multifunctional properties of C-peptide may open up new avenues for therapeutic interventions in various medical specialties.
By delving into the diverse functions of C-peptide, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may lead to innovative approaches for diabetes management and offer insights into the broader healthcare implications of C-peptide.

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

Description:

Human GLP-2

GLP2, GLP-2, GLP 2.

Product # :

HOR-305

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Description

GLP-2 contains 34 amino acids having a molecular mass of 3922.35 Dalton.

Formulation

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

Purity

Greater than 98.0% as determined by RP-HPLC.

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Introduction
GLP-2 functions as an intestinal growth factor, which stimulates intestinal epithelial growth. GLP2 is involved in diabetes-associated bowel growth. GLP2 enhances cell differentiation, playing a role as a cytokine and in tissue regeneration, and mediating cytoprotection. GLP2 is invloded numerous therapeutic applications. GLP2 regulates signaling pathways coupled to cell proliferation and cell death by apoptosis.
GLP-2 is produced by specific post-translational proteolytic cleavage of proGLP. GLP-2 is manufactured by the intestinal endocrine L cell and by several neurons in the central nervous system.
Synonyms
GLP2, GLP-2, GLP 2, Glucagon Like Peptide-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GLP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLP2 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 GLP-2 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
His-Ala-Asp-Gly-Ser-Phe-Ser-Asp-Glu-Met-Asn-Thr-Ile-Leu-Asp-Asn-Leu-Ala-Ala-Arg-Asp-Phe-Ile-Asn-Trp-Leu-Ile-Gln-Thr-Lys-Ile-Thr-Asp-Arg.
Background
What is the molecular weight/Mw of GLP 2 HUMAN Protein?
GLP 2 HUMAN Protein has a total Mw of 3.92kDa.

What is the Purity of GLP 2 HUMAN Protein?
GLP 2 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GLP 2 HUMAN Protein?
The biological functionality of GLP 2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of GLP 2 HUMAN Protein?
His-Ala-Asp-Gly-Ser-Phe-Ser-Asp-Glu-Met-Asn-Thr-Ile-Leu-Asp-Asn-Leu-Ala-Ala-Arg-Asp-Phe-Ile-Asn-Trp-Leu-Ile-Gln-Thr-Lys-Ile-Thr-Asp-Arg.

What applications can GLP 2 HUMAN Protein be used in?
GLP 2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GLP 2 HUMAN Protein?
The endotoxin level is minimal, GLP 2 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:

Growth Hormone Releasing Peptide-4

GHRP-4, GHRP4.

Product # :

HOR-022

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Description

Growth Hormone Releasing Peptide-4 Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 607.73 Dalton and a Molecular formula of C34H37N7O4.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Introduction
GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH effect on pituitary somatotrophs to stimulate GH release. The GHRP4 is one of several synthetic met-enkephalin analogs that owns unnatural D-amino acids. They were developed for their growth hormone (GH) releasing activity and called GH secretatogues. They lack opioid activity but are potent stimulators of GH release. These secretatogues are distinct from the growth hormone releasing hormone (GHRH or GHRF) as they share no sequence relation and derive their function through action at a completely different receptor, the ghrelin receptor.
Synonyms
GHRP-4, GHRP4.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Growth Hormone Releasing Peptide-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHRP4 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 GHRP4 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
(D-Trp)-Ala-Trp-(D-Phe)-NH2.
Background
What is the molecular weight/Mw of GHRP4 Protein?
GHRP4 Protein has a total Mw of 0.607kDa.

What is the Purity of GHRP4 Protein?
GHRP4 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of GHRP4 Protein?
The biological functionality of GHRP4 Protein will be determined in the future.

What is the amino acid sequence of GHRP4 Protein?
(D-Trp)-Ala-Trp-(D-Phe)-NH2.

What applications can GHRP4 Protein be used in?
GHRP4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GHRP4 Protein?
The endotoxin level is minimal, GHRP4 Protein was purified using conventional chromatography techniques.

Who supplies GHRP4 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of GHRP4?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Fertirelin

Product # :

HOR-037

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Description

Fertirelin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1153.31 Dalton and a Molecular formula of C55H76N16O12.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Fertirelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fertirelin 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 Fertirelin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-NHEt.
Background
Fertirelin, a potent gonadotropin-releasing hormone (GnRH) analogue, is crucial for fertility regulation in animals. This research paper endeavors to expound on the biochemical attributes of fertirelin and its potential therapeutic applications in veterinary medicine.
Fertirelin, a synthetic analogue of the natural gonadotropin-releasing hormone, plays a fundamental role in fertility regulation in veterinary medicine. It stimulates the secretion of luteinizing hormone and follicle-stimulating hormone, crucial for reproduction (Kotwica et al., 2005). This paper aims to delve into the biochemical characteristics of fertirelin and its potential applications.
Fertirelin, as a GnRH analogue, elicits its action by binding to GnRH receptors located on pituitary gonadotroph cells. This leads to the release of luteinizing hormone and follicle-stimulating hormone, key players in ovulation and spermatogenesis (Kotwica et al., 2005).
In the realm of veterinary medicine, fertirelin is primarily used for treating ovarian follicular cysts in dairy cattle (Bosu & Peter, 1987). Its potent stimulatory effect on gonadotropin secretion facilitates ovulation and contributes to fertility management strategies.
The potential of fertirelin extends beyond the current applications. Further research into the precise mechanism of action and potential side effects can enhance its utilization. Overall, fertirelin presents a powerful tool in veterinary reproductive medicine, making it a focal point of interest for future studies.
What is the molecular weight/Mw of FERTIRELIN Protein?
FERTIRELIN Protein has a total Mw of 1.15kDa.

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

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

What is the amino acid sequence of FERTIRELIN Protein?
Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-NHEt.

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

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

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

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

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

Description:

Bremelanotide

PT-141, Rekynda, bremelanotide acetate.

Product # :

HOR-039

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Description

Bremelanotide Synthetic is a single, non-glycosylated polypeptide chain containing 6 amino acids, having a molecular mass of 1025.16 Dalton and a Molecular formula of C50H68N40O10.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Synonyms
PT-141, Rekynda, bremelanotide acetate.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Bremelanotide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bremelanotide 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 Bremelanotide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Ac-Nle-cyclo(-Asp-His-D-Phe-Arg-Trp-Lys)-OH.
Background
Bremelanotide (PT-141), a synthetic heptapeptide, is a novel therapeutic agent primarily utilized for the treatment of sexual dysfunction. This paper provides an exhaustive review of Bremelanotide, detailing its biochemical structure, mechanism of action, therapeutic applications, and future prospects in clinical medicine.
Bremelanotide (PT-141), derived from Melanotan II, is a synthetic peptide developed for its role in treating sexual dysfunction in both men and women (Clayton et al., 2016). This paper presents a comprehensive examination of Bremelanotide, its biological properties, and potential therapeutic uses.
Bremelanotide acts as a non-selective agonist of the melanocortin receptors, primarily MC3R and MC4R, present in the central nervous system. The peptide initiates its action in the hypothalamus, leading to downstream effects on sexual desire and arousal (King et al., 2007).
The US Food and Drug Administration approved Bremelanotide for the treatment of premenopausal women with hypoactive sexual desire disorder (HSDD) in 2019. In clinical trials, it demonstrated efficacy in enhancing sexual desire and reducing distress associated with HSDD (Kingsberg et al., 2019).
While the current focus of Bremelanotide is on treating sexual dysfunction, its future potential may extend to other areas due to its unique mechanism of action. Further research is needed to explore the full therapeutic potential of this intriguing peptide. In conclusion, Bremelanotide represents a significant advance in sexual dysfunction therapeutics, with potential implications extending beyond this realm.

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:

Resistin Rat Recombinant

Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

Product # :

CYT-1129

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Description

Resistin Rat Recombinant produced in E.Coli is disulfide-linked homodimer consisting of 2x95 amino acid polypeptide chains and having a molecular mass of approximately 20.2kDa.Resistin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20.

Purity

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

More Info

Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belongs to the class of cysteine-rich secreted proteins (monomeric peptide contains 11 cysteine residues) referred to as the RELM family, and is also described as ADSF (Adipose Tissue-Specific Secretory Factor) or FIZZ3 (Found in Inflammatory Zone 3). Resistin may be an important link between obesity. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppressed the ability to stimulate glucose uptake. They have also suggested that resistin was present at elevated levels in blood of obese mice, and was down regulated by fasting and by antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.
Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin 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 Resistin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MPSMSLCPMD EAISKKINQD FSSLLPAAMK NTVLHCWSVS SRGRLASCPE GTTVTSCSCG SGCGSWDVRE DTMCHCQCGS IDWTAARCCT LRVGS.

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:

Secreted Phospholipase A2-X Human Recombinant

Group 10 secretory phospholipase A2, EC 3.1.1.4, Group X secretory phospholipase A2, Phosphatidylcholine 2-acylhydrolase GX, GX sPLA2, sPLA2-X, SPLA2, GXPLA2, MGC119918, MGC119919, MGC133367, PLA2G10.

Product # :

ENZ-329

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Description

Secreted Phospholipase A2-X Human Recombinant is manufactured with N-terminal fusion HisTag. PLA2G10 His-Tagged Fusion Protein, is 15.5 kDa containing 123 amino acid residues of the human secreted phospholipase A2-X and 16 additional amino acid residues - HisTag (underlined).

Source

Escherichia Coli.

Formulation

PLA2G10 filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 20mM Tris and 50mM NaCl, pH 7.5.

Purity

Greater than 95% as determined by SDS PAGE.

More Info

Introduction
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso-PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.
Synonyms
Group 10 secretory phospholipase A2, EC 3.1.1.4, Group X secretory phospholipase A2, Phosphatidylcholine 2-acylhydrolase GX, GX sPLA2, sPLA2-X, SPLA2, GXPLA2, MGC119918, MGC119919, MGC133367, PLA2G10.
Physical Appearance
Sterile Filtered 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.
Amino Acid Sequence
MRGSHHHHHH GMASHMGILE LAGTVGCVGP RTPIAYMKYG CFCGLGGHGQ PRDAIDWCCH GHDCCYTRAE EAGCSPKTER YSWQCVNQSV LCGPAENKCQ ELLCKCDQEI ANCLAQTEYN LKYLFYPQFL CEPDSPKCD

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

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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:

Procalcitonin Porcine Recombinant

Calcitonin, Preprocalcitonin, Calca.

Product # :

HOR-018

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Quantity :

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Description

Procalcitonin Porcine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Thr26-Asn141) containing 126 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 14.1kDa.

Source

Escherichia Coli.

Formulation

Procalcitonin was filtered (0.4µm) and lyophilized in 20mM TRIS and 50mM NaCl, pH 8.0.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
Synonyms
Calcitonin, Preprocalcitonin, Calca.
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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHASTPLRSALETL PDPGPLSEKE GRLLLAALVK AYVQRKTNEL EQEQEQETEG SSLDSSRAKR CSNLSTCVLS AYWRNLNNFH RFSGMGFGPE TPGKKSDIAS SLERDLFPRG MPQDAN.
Background
What is the molecular weight/Mw of PROCALCITONIN PORCINE Protein?
PROCALCITONIN PORCINE Protein has a total Mw of 14.1kDa.

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

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

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

What is the amino acid sequence of PROCALCITONIN PORCINE Protein?
MKHHHHHHASTPLRSALETL PDPGPLSEKE GRLLLAALVK AYVQRKTNEL EQEQEQETEG SSLDSSRAKR CSNLSTCVLS AYWRNLNNFH RFSGMGFGPE TPGKKSDIAS SLERDLFPRG MPQDAN.

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

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

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

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

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

Description:

Serine Peptidase Inhibitor Kazal Type 1 Human Recombinant

Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.

Product # :

ENZ-724

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Description

SPINK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 79 amino acids (24-79) and having a molecular mass of 8.6kDa.SPINK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SPINK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
Trypsin inhibitor SPINK1 is secreted from pancreatic acinar cells into pancreatic fluid. SPINK1 has a role in inhibition of trypsin-catalyzed premature initiation of zymogens in the pancreas and the pancreatic duct. Alterations in SPINK1 gene are the cause for tropical calcific and pancreatitis hereditary pancreatitis.
Synonyms
Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.
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 MGSDSLGREA KCYNELNGCT KIYDPVCGTD GNTYPNECVL CFENRKRQTS ILIQKSGPC.

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:

ProInsulin C-Peptide Analogue Human Recombinant

Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.

Product # :

CYT-1120

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
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Description

ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.ProInsulin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

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Introduction
Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Synonyms
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized ProInsulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProInsulin C-Peptide Analogue 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 ProInsulin C-Peptide Analogue in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR.

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:

Survodutide

Product # :

HOR-061

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Survodutide is a synthetic single, non-glycosylated polypeptide chain containing 29 amino acids, having a molecular mass of 4231.62 Dalton and a Molecular formula of C192H289N47O61.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Survodutide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Survodutide 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 Survodutide 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-1-Aminocyclobutanecarboxylic acid-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Glu-ArgAla-Ala-Lys-Asp-Phe-Ile-Lys-(Gly-Gly-Ser-Gly-Ser-Gly-γ-Gludiacid18)-Trp-Leu-Glu-Ser-Ala-NH2.
Background
Survodutide is a dual agonist targeting both the GLP-1 and Glucagon receptors. It has a glucagon component, which effects directly on the liver to increase energy expenditure and clear fat. Survodutide takes part in treatment of liver disease, mainly Metabolic Dysfunction-Associated Steatohepatitis, while simultaneously advancing through Phase 3 trials for obesity.

What is the molecular weight/Mw of SURVODUTIDE Protein?
SURVODUTIDE Protein has a total Mw of 4.231kDa.

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

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

What is the amino acid sequence of SURVODUTIDE Protein?
H-His-1-Aminocyclobutanecarboxylic acid-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Glu-ArgAla-Ala-Lys-Asp-Phe-Ile-Lys-(Gly-Gly-Ser-Gly-Ser-Gly-γ-Gludiacid18)-Trp-Leu-Glu-Ser-Ala-NH2.

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

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

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

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

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

Description:

Secreted Phospholipase A2-XII Human Recombinant

Group XIIA secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GXII, GXII sPLA2, PLA2G12, sPLA2-XII, PLA2G12A.

Product # :

ENZ-330

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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description
source
formulation
purity
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Description

Secreted Phospholipase A2-XII Human Recombiannt was produced with N-terminal His-Tag. PLA2G12 His-Tagged Fusion Protein is 20.6 kDa containing 167 amino acid residues of the human secreted phospholipase A2-XII and 16 additional amino acid residues – His-Tag (underlined).

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.01M Tris buffer pH 8.6.

Purity

Greater than 95% as determined by SDS PAGE.

More Info

Introduction
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
The secretory PLA2 (sPLA2) family, in which 10 isozymes have been identified, consists of low molecular weight, Ca2+-requiring secretory enzymes that have been implicated in a number of biological processes, such as modification of eicosanoid generation, inflammation, and host defense.
This enzyme has been proposed to hydrolyze phosphatidylcholine (PC) in lipoproteins to liberate lyso- PC and free fatty acids in the arterial wall, thereby facilitating the accumulation of bioactive lipids and modified lipoproteins in atherosclerotic foci.
In mice, sPLA2 expression significantly influences HDL particle size and composition and demonstrate that an induction of sPLA2 is required for the decrease in plasma HDL cholesterol in response to inflammatory stimuli. Instillation of bacteria into the bronchi was associated with surfactant degradation and a decrease in large:small ratio of surfactant aggregates in rats.
Synonyms
Group XIIA secretory phospholipase A2, EC 3.1.1.4, Phosphatidylcholine 2-acylhydrolase GXII, GXII sPLA2, PLA2G12, sPLA2-XII, PLA2G12A.
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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Amino Acid Sequence
MRGSHHHHHH GMASHMQEQA QTTDWRATLK TIRNGVHKID TYLNAALDLL GGEDGLCQYK CSDGSKPFPR YGYKPSPPNG CGSPLFGVHL NIGIPSLTKC CNQHDRCYET CGKSKNDCDE EFQYCLSKIC RDVQKTLGLTQ HVQACETTVE LLFDSVIHLG CKPYLDSQRA ACRCHYEEKT DL
Applications
Western blotting.

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

Description:

Growth Hormone Releasing Peptide-5

GHRP-5, GHRP5.

Product # :

HOR-023

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Growth Hormone Releasing Peptide-5 Synthetic is a single, non-glycosylated polypeptide chain containing 5 amino acids, having a molecular mass of 770.91 Dalton and a Molecular formula of C43H46N8O6.

Formulation

The protein was lyophilized with no additives.

Purity

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

More Info

Introduction
GH-releasing peptides (GHRPs) are synthetic peptides that like GHRH effect on pituitary somatotrophs to stimulate GH release. The GHRP5 is one of several synthetic met-enkephalin analogs that owns unnatural D-amino acids. They were developed for their growth hormone (GH) releasing activity and called GH secretatogues. They lack opioid activity but are potent stimulators of GH release. These secretatogues are distinct from the growth hormone releasing hormone (GHRH or GHRF) as they share no sequence relation and derive their function through action at a completely different receptor, the ghrelin receptor.
Synonyms
GHRP-5, GHRP5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Growth Hormone Releasing Peptide-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GHRP5 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 GHRP5 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Tyr-(D-Trp)-Ala-Trp-(D-Phe)-NH2.
Background
What is the molecular weight/Mw of GHRP5 Protein?
GHRP5 Protein has a total Mw of 0,770kDa.

What is the Purity of GHRP5 Protein?
GHRP5 Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of GHRP5 Protein?
The biological functionality of GHRP5 Protein will be determined in the future.

What is the amino acid sequence of GHRP5 Protein?
Tyr-(D-Trp)-Ala-Trp-(D-Phe)-NH2.

What applications can GHRP5 Protein be used in?
GHRP5 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GHRP5 Protein?
The endotoxin level is minimal, GHRP5 Protein was purified using conventional chromatography techniques.

Who supplies GHRP5 that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of GHRP5?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Glucagon Receptor Human Recombinant

GL-R, GLR, Glucagon Receptor.

Product # :

HOR-020

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
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purity
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Description

GCGR Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain (a.a 29-142) containing 125 amino acids including an 8 a.a C-terminal His tag. The total molecular mass is 19.9kDa (calculated).

Source

E. coli

Formulation

GCGR filtered (0.4 µm) and lyophilized from solution in acetonitrile/0,1%TFA and 1% (w/v) trehalose.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Glucagon receptor is part of the glucagon receptor family which also contains GLP-1, GLP-2, GHRH and GIP receptors. GCGR regulates blood glucose levels and is mainly expressed in the pancreas, liver and kidneys. Mutations in GCGR are a cause of non-insulin-dependent diabetes mellitus.
Synonyms
GL-R, GLR, Glucagon Receptor.
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 one week 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. GCGR is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MQVMDFLFEK WKLYGDQCHH NLSLLPPPTE LVCNRTFDKY SCWPDTPANT TANISCPWYL PWHHKVQHRF VFKRCGPDGQ WVRGPRGQPW RDASQCQMDG EEIEVQKEVA KMYSSFQLEH HHHHH.
Background
What is the molecular weight/Mw of GLUCAGON RECEPTOR Protein?
GLUCAGON RECEPTOR Protein has a total Mw of 19.9kDa.

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

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

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

What is the amino acid sequence of GLUCAGON RECEPTOR Protein?
MQVMDFLFEK WKLYGDQCHH NLSLLPPPTE LVCNRTFDKY SCWPDTPANT TANISCPWYL PWHHKVQHRF VFKRCGPDGQ WVRGPRGQPW RDASQCQMDG EEIEVQKEVA KMYSSFQLEH HHHHH.

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

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

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

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

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

Description:

Glucagon Human

GLP1, GLP2, GRPP.

Product # :

HOR-286

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
purity
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Description

Glucagon Human Synthetic is a single, non-glycosylated, polypeptide chain containing 29 amino acids and having a molecular mass of 3483 Dalton and the molecular formula is: C153H225N43O49S.The Glucagon is purified by proprietary chromatographic techniques.

Formulation

Glucagon peptide was formulated with no additives.

Purity

Greater than 98.0% as determined by RP-HPLC.

More Info

Introduction
Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (?-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract.
Synonyms
GLP1, GLP2, GRPP.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Glucagon although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Glucagon 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 Glucagon in a sterile 1% HCl solution at a concentration of 0.1-1 mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
H-His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-OH.HCL
Background
What is the molecular weight/Mw of GLUCAGON Protein?
GLUCAGON Protein has a total Mw of 3.483kDa.

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

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

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

What is the amino acid sequence of GLUCAGON Protein?
H-His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-OH. HCL

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

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

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

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

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

Description:

Thyroid Stimulating Hormone Human

Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.

Product # :

HOR-001

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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source
formulation
purity
biological activity
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Description

Thyroid Stimulating Hormone Human produced in Human pituitary glands is an important indicator of thyroid function.

Source

Human pituitary glands

Formulation

Lyophilized from a concentrated solution containing 50mM ammonium bicarbonate.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

11.72 IU/mg vial by Centaur CP. Siemens Centaur CP is standardized against WHO 3rd IRP 81/565.

More Info

Introduction
Thyroid-stimulating hormone (also known as TSH or thyrotropin) is a hormone synthesized and secreted by thyrotrope cells in the anterior pituitary gland which regulates the endocrine function of the thyroid gland.
TSH stimulates the thyroid gland to secrete the hormones thyroxine (T4) and triiodothyronine (T3). TSH production is controlled by a Thyrotropin Releasing Hormone, (TRH), which is manufactured in the hypothalamus and transported to the Anterior Pituitary gland, where it increases TSH production and release. Somatostatin is also produced by the hypothalamus, and has an opposite effect on the pituitary production of TSH, decreasing or inhibiting its release.
The level of Thyroid hormones (T3 and T4) in the blood have an additional effect on the pituitary release of TSH, When the levels of T3 and T4 are low, the production of TSH is increased, and conversely, when levels of T3 and T4 are high, then TSH production is decreased. This effect creates a regulatory negative feedback loop.
TSH is a glycoprotein and consists of two subunits, the alpha and the beta subunit.
The a (alpha) subunit is identical to that of human chorionic gonadotropin (HCG), luteinising hormone (LH), follicle-stimulating hormone (FSH).
The b (beta) subunit is unique to TSH, and therefore determines its function.
Synonyms
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSH 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 TSH in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the source or expression system of TSH HUMAN Protein?
Human pituitary glands

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

What is the Biological Activity of TSH HUMAN Protein?
11.72 IU/mg vial by Centaur CP. Siemens Centaur CP is standardized against WHO 3rd IRP 81/565.

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

What is the endotoxin level for TSH HUMAN Protein?
The endotoxin level is minimal, TSH 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.

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