Search: 1000 results found for "Selectin"

Description:

Leptin Dog Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-506

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Description

Leptin Dog 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 0.02% NaHCO3.

Purity

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

Biological Activity

Biological active as 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 0.4% NaHCO3 adjusted to 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-Arg.
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:

Humanin

Product # :

HOR-042

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Description

Humanin Synthetic is a single, non-glycosylated polypeptide chain containing 24 amino acids, having a molecular mass of 2687 Dalton and a Molecular formula of C119H204N34O32S2 .

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 Humanin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Humanin 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 Humanin 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-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala-OH.
Background
Humanin, a small peptide derived from the mitochondrial genome, has emerged as a remarkable molecule with diverse cellular protective functions. This research paper aims to provide a comprehensive analysis of Humanin, exploring its biochemical properties, mechanisms of action, and potential therapeutic applications in various disease contexts.
Humanin, initially discovered for its role in neuroprotection, has since garnered interest for its broad spectrum of cytoprotective effects. Derived from the mitochondrial 16S ribosomal RNA, this small peptide plays a critical role in safeguarding cells from various stressors (Harvey, 2008). This paper delves into the complexities of Humanin, uncovering its multifaceted nature and potential clinical applications.
Humanin is a 24-amino acid peptide with a unique secondary structure that contributes to its cellular protective functions. It localizes to both the cytoplasm and mitochondria, where it interacts with various proteins involved in apoptotic and oxidative stress pathways (Hoang et al., 2019). Additionally, Humanin can undergo post-translational modifications, further diversifying its actions.
Humanin exerts its protective effects through multiple mechanisms. It interacts with the pro-apoptotic protein Bax, inhibiting its translocation to the mitochondria and preventing the release of cytochrome c (Hashimoto et al., 2001). Humanin also modulates the activities of caspases, key mediators of cell death pathways, thereby promoting cell survival in stressful conditions (Nakagawa et al., 2002).
Beyond its initial recognition as a neuroprotective agent, Humanin has demonstrated cytoprotective effects in various cell types, including cardiomyocytes, neurons, and endothelial cells (Chai et al., 2019). It attenuates oxidative stress, reduces mitochondrial dysfunction, and promotes cell viability, thereby safeguarding cells from a multitude of insults.
The multifaceted protective functions of Humanin offer promising therapeutic potential in various disease contexts. Research has shown its efficacy in mitigating neurodegenerative disorders, cardiovascular diseases, and age-related pathologies (Muzumdar et al., 2009). Furthermore, Humanin's ability to attenuate inflammation and promote tissue repair opens new avenues for therapeutic interventions.

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:

Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-018

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Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

Purity

Greater than 95.0% as determined by SEC-HPLC.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Colorless, clear and transparent solution.
Stability
G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.
Background
What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

What is the source or expression system of G CSF HUMAN, PEG Protein?
Escherichia Coli.

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

What is the Biological Activity of G CSF HUMAN, PEG Protein?
The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

What is the amino acid sequence of G CSF HUMAN, PEG Protein?
G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

What is the endotoxin level for G CSF HUMAN, PEG Protein?
The endotoxin level is minimal, G CSF HUMAN, PEG 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:

Cytokine Induced Apoptosis Inhibitor 1 Human Recombinant

DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.

Product # :

PRO-024

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Description

CIAPIN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-312 a.a.) and having a molecular mass of 36kDa.CIAPIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CIAPIN1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Anamorsin, ( CIAPIN) is a member of anamorsin family. CIAPIN mainly expressed in the cytoplasm of liver, pancreas and heart tissue cells and does not show any homology to known apoptosis regulatory molecules of the Bcl-2 or CASP families, or to signal transduction molecules. CIAPIN1 Expression is reliant on growth factor stimulation. It is a ubiquitously expressed protein, and when it is overexpressed, it grants apoptotic resistance.
Synonyms
DRE2, PRO0915, Anamorsin, Cytokine-induced apoptosis inhibitor 1, Fe-S cluster assembly protein DRE2 homolog, CIAPIN1.
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 MGSMADFGIS AGQFVAVVWD KSSPVEALKG LVDKLQALTG NEGRVSVENI KQLLQSAHKE SSFDIILSGL VPGSTTLHSA EILAEIARIL RPGGCLFLKE PVETAVDNNS KVKTASKLCS ALTLSGLVEV KELQREPLTP EEVQSVREHL GHESDNLLFV QITGKKPNFE VGSSRQLKLS ITKKSSPSVK PAVDPAAAKL WTLSANDMED DSMDLIDSDE LLDPEDLKKP DPASLRAASC GEGKKRKACK NCTCGLAEEL EKEKSREQMS SQPKSACGNC YLGDAFRCAS CPYLGMPAFK PGEKVLLSDS NLHDA.

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:

Gliadin Triticum Aestivum Grain Native

Product # :

PRO-2675

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Description

The native Gliadin Triticum Aestivum Grain is purified from wheat by protein chemical methods.

Formulation

Gliadin is supplied in 20mM HEPES buffer pH-7.4 and 6M Urea.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Gliadin is a common substrate of transglutaminase, which generates neo-epitopes by deamidation of glutamine side chains. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.
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. Avoid multiple freeze-thaw cycles.
Immunological Functions
1. Binds IgG and IgA-type human auto antibodies in sera of patients diagnosed with celiac disease.2. Immunodot analysis with positive/negative samples.
Applications
Western blot with patient sample.

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:

Clusterin Canine Recombinant

CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Glycoprotein 80, Gp80, CLU, Clusterin, Apolipoprotein J, Apo-J.

Product # :

CYT-549

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Description

Apolipoprotein-J canine Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain (Asn227~Glu445) and having a molecular mass of 30 kDa.
The protein is fused to His tag at N-Terminus.
The Apolipoprotein-J canine is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Canine Clusterin was lyophilized from 20mM Tris, 150mM NaCl, pH8.0, 0.01% skl and 5%Trehalose.

Purity

Greater than 90% as determined by SDS PAGE.

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Introduction
Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.
Synonyms
CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Glycoprotein 80, Gp80, CLU, Clusterin, Apolipoprotein J, Apo-J.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Reconstitute in 20mM Tris and 150mM NaCl (pH8.0) to a concentration of 0.1-1.0 mg/mL and let the lyophilized pellet dissolve completely.
Amino Acid Sequence
NIIPFP RFQPLNFHDM FQPFFDMIHQ AQQAMDVNLH RIPYHFPIEF PEEDNRTVCK EIRHNSTGCL KMKDQCEKCQ EILSVDCSSN NPAQVQLRQE LSNSLQIAEK FTKLYDELLQ SYQEKMFNTS SLLKQLNEQF SWVSQLANLT QSEDPFYLQV TTVGSQTSDS NVPVGFTKVV VKLFDSDPIT VMIPEAVSRN NPKFMETVAE KALQEYRQKHREE.
Background
What is the molecular weight/Mw of CLUSTERIN Protein?
CLUSTERIN Protein has a total Mw of 30kDa.

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

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

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

What is the amino acid sequence of CLUSTERIN Protein?
NIIPFP RFQPLNFHDM FQPFFDMIHQ AQQAMDVNLH RIPYHFPIEF PEEDNRTVCK EIRHNSTGCL KMKDQCEKCQ EILSVDCSSN NPAQVQLRQE LSNSLQIAEK FTKLYDELLQ SYQEKMFNTS SLLKQLNEQF SWVSQLANLT QSEDPFYLQV TTVGSQTSDS NVPVGFTKVV VKLFDSDPIT VMIPEAVSRN NPKFMETVAE KALQEYRQKHREE.

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

What is the endotoxin level for CLUSTERIN Protein?
The endotoxin level is minimal, CLUSTERIN 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

FST, FS

Product # :

CYT-232

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Description

Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

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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 functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
Synonyms
FST, FS
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin 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 Gly-Asn-Cys-Trp-Leu.
Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.

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

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

What is the Biological Activity of FOLLISTATIN HUMAN Protein?
The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.

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

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

Adiponectin Globular Recombinant, His Tag

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-277

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Description

Acrp30 Human has a total of 171 amino acids. N-terminal underlined amino acids are His-tag and the protease cleavage site (31AA-Underlined). The AA sequence of Acrp30 Human is homologous to the 105-244 amino acid sequence of the Human full-length Adiponectin (Swiss-prot entry Q15848).

Source

Escherichia Coli.

Formulation

Acrp30 Human is a filtered powder, lyophilized from 0.6mg/ml in PBS buffer.

Purity

Purity of Acrp30 Human is greater than 95% as determined by SDS PAGE.

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Introduction
Adiponectin is a protein exclusively secreted from adipose tissue. In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (LMW, also called trimer) forms. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Stability
For long term, store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. The lyophilized Acrp30 Human remains stable for 24 months when stored at -20°C.
Solubility
Add deionized water and let the lyophilized pellet of Acrp30 Human dissolve completely.
Amino Acid Sequence
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.7kDa.

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

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.

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

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

Adiponectin Human Recombinant, His tag

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-433

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

The Acrp30 Human is created as a recombinant protein with N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is 26.4 kDa protein containing 230 amino acid residues of the Acrp30 Human and 12 additional amino acid residues - HisTag (underlined).

Source

Escherichia Coli.

Formulation

Acrp30 Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.02M Tris buffer pH7.5, 0.15M NaCl.

Purity

Acrp30 Human purity is greater than 95% as determined by SDS-PAGE.

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Introduction
Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human 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
MRGSHHHHHHGSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD TN.
Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 26.4kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
MRGSHHHHHHGSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD TN.

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

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

Adiponectin Mouse Recombinant, His Tag

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-537

Price :

Quantity :

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Description

The Adiponectin Mouse is created as a recombinant protein with a 21 a.a N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is a 27.2kDa protein containing 251 amino acid residues of the Acrp30 Mouse, 18-247 amino acids.

Source

Escherichia Coli.

Formulation

Acrp30 Mouse is a sterile filtered liquid formulation containing (1mg/ml) 20mM Tris-HCl pH-8, 1mM DTT and 10% Glycerol.

Purity

Acrp30 Mouse purity is greater than 90% as determined by SDS-PAGE.

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Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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 MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 27.2kDa.

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

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
MGSSHHHHHH SSGLVPRGSH MEDDVTTTEE LAPALVPPPK GTCAGWMAGI PGHPGHNGTP GRDGRDGTPG EKGEKGDAGL LGPKGETGDV GMTGAEGPRG FPGTPGRKGE PGEAAYVYRS AFSVGLETRV TVPNVPIRFT KIFYNQQNHY DGSTGKFYCN IPGLYYFSYH ITVYMKDVKV SLFKKDKAVL FTYDQYQEKN VDQASGSVLL HLEVGDQVWL QVYGDGDHNG LYADNVNDST FTGFLLYHDT N.

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

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

Semenogelin I Human Recombinant

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

Product # :

PRO-1732

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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:

Leptin Antagonist Quadruple Mutant Human Recombinant

Product # :

CYT-353

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Description

Leptin Quadruple Mutant Human Recombinant is a single polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a Mw of 16 kDa, Human Leptin was mutated, resulting in L39A/D40A/F41A/I42A.Leptin Antagonist Quadruple Mutant was 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 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

ProSpec’s Leptin Quadruple Antagonist Mutant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transected 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 Quadruple Mutant 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 Quadruple Mutant in sterile 0.4% NaHCO3 adjusted to 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 0.89 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:

Nucleobindin-2 Human Recombinant

Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

Product # :

PRO-492

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Description

The Recombinant Human NUCB2 (Nesfatin) produced in E.coli has a molecular mass of 9.7kDa containing 82 amino acid residues of the human NUCB2.

Source

Escherichia Coli.

Formulation

The NUCB2 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×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
Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.
Synonyms
Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NUCB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NUCB2 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 NUCB2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL.

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 Triple Antagonist (D23L) Pegylated Mouse Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-1242

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Description

Leptin Antagonist Triple Mutant D23L Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus. The 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 D23L Mouse Recombinant is capable of stimulating proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated recombinant mouse leptin but in vivo it has profound weight reducing effect (as compared to the non-pegylated recombinant mouse leptin), resulting mainly from reduced food intake.

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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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 > 0.1mg/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% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
Background
Leptin is a hormone which mainly produced by adipocytes . Leptin’s main part is to regulate long-term energy balance. Leptin 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:

Cathelicidin Antimicrobial Peptide Human Recombinant

CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.

Product # :

PRO-1405

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Description

CAMP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (34-173 a.a.) and having a molecular mass of 18.4kDa.CAMP is fused to a 23 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

CAMP protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
CAMP belongs to the antimicrobial peptide family, contains highly conserved N-terminal signal peptide, a cathelin domain and a structurally variable cationic antimicrobial peptide that produced by extracellular proteolysis from the C-terminus. CAMP has numerous functions besides the antimicrobial activity such as: cell chemotaxis, immune mediator induction and inflammatory response regulation.
Synonyms
CAP-18, CAP18, CRAMP, FALL-39, FALL39, HSD26, LL37, 18 kDa cationic antimicrobial protein, FALL-39 peptide antibiotic, Cathelicidin antimicrobial peptide.
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 MGSQVLSYKE AVLRAIDGIN QRSSDANLYR LLDLDPRPTM DGDPDTPKPV SFTVKETVCP RTTQQSPEDC DFKKDGLVKR CMGTVTLNQA RGSFDISCDK DNKRFALLGD FFRKSKEKIG KEFKRIVQRI KDFLRNLVPR TES.

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.

Description:

Adiponectin (72-244) Human Recombinant

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-1231

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Description

The Adiponectin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E. coli, is a 24kDa protein containing 173 amino acid residues of the Acrp30 Human, 72-244 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.

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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Adiponectin 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
IGPKGDI GETGVPGAEG PRGFPGIQGR KGEPGEGAYV YRSAFSVGLE TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF HCNIPGLYYF AYHITVYMKD VKVSLFKKDK AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY HDTN
Background
Adiponectin is a protein produced and secreted by adipose tissue. Adiponectin takes part in regulating glucose levels as well as fatty acid breakdown.
Adiponectin ‘s Functions:
Anti-Inflammatory Effects - Adiponectin has anti-inflammatory properties that helps mitigate chronic inflammation.
Regulation of Glucose and Lipid Metabolism - Adiponectin Enhances insulin sensitivity, helping in regulation of blood sugar levels and also promotes fatty acid oxidation, which helps reduce fat accumulation.
Cardiovascular Health - It may influence vascular health and is associated with a lower risk of cardiovascular diseases.
Levels and Health Implications:
Normal Levels - usually, higher levels of adiponectin are associated with a lower risk of metabolic syndrome, cardiovascular diseases and type 2 diabetes.
Low Levels - Reduced adiponectin levels are often linked with obesity, insulin resistance, and other metabolic disorders.
Factors Influencing on the Adiponectin Levels:
Weight - High body fat (especially visceral fat) can lower adiponectin levels.
Diet and Exercise - Regular physical activity and a healthy diet can increase adiponectin levels.
Genetics - Genetic factors might also be an influence on an individual adiponectin level.
Adiponectin is an important component in metabolic health, therefore continuing the research of its functions and regulation keeps advance our understanding of its role in diseases like diabetes and cardiovascular conditions.
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
IGPKGDI GETGVPGAEG PRGFPGIQGR KGEPGEGAYV YRSAFSVGLE TYVTIPNMPI RFTKIFYNQQ NHYDGSTGKF HCNIPGLYYF AYHITVYMKD VKVSLFKKDK AMLFTYDQYQ ENNVDQASGS VLLHLEVGDQ VWLQVYGEGE RNGLYADNDN DSTFTGFLLY HDTN.

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

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

Globular Adiponectin Mouse Recombinant

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-432

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Description

The globular domain of Adiponectin Mouse Recombinant / Acrp30 Mouse contains 138 amino acid residues from a.a. 111-247 having molecular mass of 16 kDa was over expressed in E.coli and purified by using conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

Acrp30 Mouse (1mg/ml) solution containing 20mM Tris-HCl pH7.5, 50mM NaCl, 5mM DTT and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Adiponectin (247amino acids) is adipocyte complement-related protein of 30 kDa and exclusively expressed in differentiated adipocytes. APM-1 (Acrp30 Mouse) is a member of the complement factor C1q family and consists of signal sequence, Non-homologous sequence, collagen domain and domain (gAcrp30).
Adiponectin expression is reduced in a variety of obese and insulin-resistant states in human, monkeys and mice. Injection of Acrp30 Mouse (247aa) or gAcrp30 (globular domain) lowers serum glucose and free fatty acid level in mice.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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
MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16kDa.

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

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

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

What is the amino acid sequence of ADIPONECTIN Protein?
MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN

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

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

Resistin Mouse Recombinant, Flag Tag

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-457

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Description

Resistin Mouse is manufactured with signal sequence of phage fd (21aa) and C-terminal fusion of flagTag (10aa). Resistin Mouse Recombinant Flag-Tagged Fusion Protein is 13.7 kDa protein containing 93 amino acid residues of the Resistin Mouse and 31 additional amino acid residues - signal sequence of phage fd, flagTag (underlined).

Source

Escherichia Coli.

Formulation

Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Resistin may be an important link between obesity resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
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
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 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 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 antigen 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
MKKLLFAIPL VVPFYSHSTM ASMPLCPIDE AIDKKIKQDF NSLFPNAIKN IGLNCWTVSS RGKLASCPEG TAVLSCSCGS ACGSWDIREE KVCHCQCARI DWTAARCCKL QVASLEDYKD DDDK.

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:

Adiponectin (108-244 a.a.) Human Recombinant

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-073

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Description

Acrp30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (108-244 a.a.) and having a molecular mass of 18.1kDa.Acrp30 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Acrp30 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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 MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN.
Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 18.1kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >80% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of ADIPONECTIN Protein? MGSSHHHHHH SSGLVPRGSH MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN..

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

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

Serglycin Human Recombinant, HEK

Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.

Product # :

PRO-2046

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Description

Serglycin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Tyr28-Leu158) containing a total of 137 amino acids, having a calculated molecular mass of 15.5kDa and fused to a 6 aa His tag at C-Terminus.

Source

HEK 293.

Formulation

SRGN filtered (0.4µm) solution in phosphate buffered saline and 20% (w/v) glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.
Synonyms
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
Physical Appearance
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
YPTRRARYQW VRCNPDSNSA NCLEEKGPMF ELLPGESNKI PRLRTDLFPK TRIQDLNRIF PLSEDYSGSG FGSGSGSGSG SGSGFLTEME QDYQLVDESD AFHDNLRSLD RNLPSDSQDL GQHGLEEDFM L 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:

Centrin-1 Human Recombinant

Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.

Product # :

PRO-1104

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Description

CETN1 Human Recombinant produced E. coli is a single polypeptide chain containing 196 amino acids (1-172) and having a molecular mass of 22.1kDa.CETN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The CETN1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
CETN1 is an EF-hand type Ca2+-binding protein. CETN1 is localized to the centrosome of interphase cells, and reorganizes the region of the spindle poles during mitosis, reflecting the dynamic behavior of the centrosome during the cell cycle. CETN1 has a vital part in the determination of centrosome position and isolation, and in the course of microtubule separating.
Synonyms
Centrin EF-hand protein 1, calcium binding protein, Caltractin isoform 2, CETN.
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 MGSHMASGFK KPSAASTGQK RKVAPKPELT EDQKQEVREA FDLFDVDGSG TIDAKELKVA MRALGFEPRK EEMKKMISEV DREGTGKISF NDFLAVMTQK MSEKDTKEEI LKAFRLFDDD ETGKISFKNL KRVANELGEN LTDEELQEMI DEADRDGDGE VNEEEFLRIM KKTSLY

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:

Fibronectin Rat

Product # :

PRO-131

Price :

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Shipping Method :

Shipped at Room temp

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Description

Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin plays a role in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion. Fibronectin consists in two main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces. Molecular Weight 220kDa.

Source

Rat Plasma.

Formulation

The Rat Fibronectin was lyophilized from a concentrated 1mg/ml solution containing 20mM Tris Cl pH-7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Store the lyophilized fibronectin at 4°C. Upon reconstitution fibronectin should be stored at 4°C for 2 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Rat Fibronectin in sterile 18M-cm H2O not less than 100µg/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:

Follistatin Human Recombinant, His Tag

FST, FS, Activin-binding protein.

Product # :

CYT-029

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Description

FST His Protein is 36.0 kDa protein containing 325 amino acid residues of the FST His and the 10 aa N-Terminal His-tag.

Source

E. coli.

Formulation

FST His Tag was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS and 20mM NaCl, pH 7.5.

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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
FST, FS, Activin-binding protein.
Stability
Store lyophilized FST His at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted FST His 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
MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.
Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN, HIS Protein?
FOLLISTATIN HUMAN, HIS Protein has a total Mw of 36kDa.

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

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

What is the amino acid sequence of FOLLISTATIN HUMAN, HIS Protein?
MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.

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

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

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

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