Search: 1000 results found for "fibrinogen"

Description:

Hepatitis C Virus Mosaic Antigen-B Recombinant

Product # :

HCV-002

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Description

HCV Mosaic-B protein contains a long core peptide residues 1-120a.a., 1192-1415a.a. of NS3, three epitopes from NS4 and two epitopes from NS5 and the genotype of all sequences are 1b. A specific peptide was identified from each region; the four peptides from each region were linked together and expressed in E .coli. The recombinant protein migrates at 65kDa.

Source

Escherichia Coli.

Formulation

HCV Mosaic-B protein solution containing 50mM arginine in PBS.

Purity

Protein is >95% pure as determined by 12% PAGE (coomassie staining).

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Introduction
Hepatitis C is one type of viral hepatitis - a liver disease - caused by the hepatitis C virus (HCV) which is usually passed through contact with infected blood but can also pass through sex with an infected person and from mother to baby during childbirth.
HCV core protein, NS3, NS4, and NS5 proteins of hepatitis C virus are all essential for detection of antibodies against HCV.
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.
Applications
ELISA, gold conjugation.

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:

Cardiac Troponin-I Human

Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

Product # :

PRO-2788

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Description

TNNI3 Native produced in Human heart tissue is a full length protein which has an additional amino acid residues on its N terminus that are not present on the skeletal form, making this protein a promising analyte for indicating cardiac specificity.TNNI3 Native is purified by proprietary chromatographic technique.

Source

Human heart tissue.

Formulation

TNNI3 was lyophilized from 0.01M HCl.

Purity

Greater than 98.0% as determined by SDS-PAGE.

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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cardiac Troponin-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 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 TNNI3 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Troponin I, encoded by the TNNI3 gene, is a critical component of the troponin complex in cardiac muscle cells. It plays a central role in the regulation of cardiac muscle contraction by modulating the interaction between actin and myosin filaments.
While extensive research has been conducted on troponin I in the context of cardiac diseases, there is a growing need to investigate native human troponin I (TNNI3) in its unmodified form to gain a deeper understanding of its functions, structural significance, and implications for heart health. This research aims to provide a comprehensive exploration of TNNI3 in its native state, shedding light on its various roles and potential applications in cardiology and biomedical research.
The primary objective of this research is to elucidate the physiological role of native human TNNI3 in cardiac muscle contraction. Experiments involving human cardiac tissue samples and isolated myocytes will be conducted to investigate how TNNI3 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of cardiac muscle physiology and its implications for heart health.
The second objective is to assess the clinical relevance of native TNNI3 in cardiac diseases. Clinical studies involving patients with various cardiac conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI3 as a biomarker. These investigations may provide valuable insights into the use of native TNNI3 in the early detection and management of heart diseases.
The third objective is to explore the potential applications of native TNNI3 in biomedical research and drug development. Research will investigate the use of native TNNI3-expressing cells as models for studying cardiac disorders and for developing novel therapeutic interventions targeting the troponin complex.
By delving into the functions and roles of native human TNNI3, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology and biomedical research.

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:

Chikungunya E1 Recombinant

Product # :

CHI-004

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Description

Recombinant Chikungunya E1 produced in E.coli having a molecular weight of 42kDa.

Source

Escherichia Coli.

Formulation

Sterile Filtered solution containing PBS and 25mM K2CO3.

Purity

Protein is >90% pure as determined by SDS-PAGE.

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Introduction
Chikungunya is an infection caused by the chikungunya virus which is passed to humans by two species of mosquito of the genus Aedes: A. albopictus and A. aegypti. Animal reservoirs of the virus include monkeys, birds, cattle, and rodents. The features of the disease are a sudden onset of fever 2-4 days after exposure. The fever typically lasts 2-7 days, while the associated joint pains usually last weeks or months but sometimes years. The mortality rate is a little less than 1 in 1,000. The disease has occurred in outbreaks in Asia, Europe and the Americas since 2004. CHIKV is a single-stranded positive-sense RNA genome, 11,800 nts long which encodes 2 open reading frames. The nucleocapsid is tightly enveloped by a host-derived lipid bilayer (envelope) supporting the virus-encoded envelope proteins. 80 glycoprotein spikes are C- terminally anchored within the viral envelope. The structural polyprotein is translated from a viral sub genomic mRNA, while as the 5 structural proteins (capsid, E3, E2, 6K, E1) are translated as a single polyprotein, from which capsid (C) is cleaved off to encapsidate. The envelope polyprotein precursor E3-E2-6K-E1 is translocated to the endoplasmatic reticulum. Polyprotein is processed by host signalases, resulting in E3, E2 & E1 forming viral hetero-trimeric spikes. The viral spikes majorly contains E2 and E1 facilitate cell receptor recognition, cell entry thru pH-dependent endocytosis and support viral budding.
Physical Appearance
Sterile filtered colorless solution.
Stability
CHIKV E1 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
PNTVGVPYKTLVNRPGYSPMVLEMELLSVTLEPTLSLDYITCEYKTVIPSPYVKCCGTAECKDKSLPDYSC
KVFTGVYPFMWGGAYCFCDTENTQLSEAHVEKSESCKTEFASAYRAHTASASAKLRVLYQGNNVTVSAY
ANGDHAVTVKDAKFIVGPMSSAWTPFDNKIVVYKGDVYNMDYPPFGAGRPGQFGDIQSRTPESEDVYAN
TQLVLQRPSAGTVHVPYSQAPSGFKYWLKERGASLQHTAPFGCQIATNPVRAMNCAVGNMPISIDIPDAAF
TRVVDAPSLTDMSCEVPACTHSSDFGGVAIIKYAASKKGKCAVHSMTNAVTIREAEIEVEGNSQLQISFSTAL
ASAEFRVQVCSTQVHCAAECHPPKDHIVNYPASHTTLGVQDISVTAMSWVQKITG
Purification Method
Purified by proprietary chromatographic technique.

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 Clusterin

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

Product # :

CYT-548

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Source

Plasma.

Formulation

Human native Clusterin was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.1M phosphate buffer, 0.15M NaCl pH 7.5.

Purity

Greater than 95% 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, Clusterin, Apolipoprotein J, Apo-J.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Clusterin 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 H2O to prepare a working stock solution of 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 in the cell culture.

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

Description:

Serpin Peptidase Inhibitor, Clade G Member 1 Human

C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

Product # :

PRO-2711

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Description

Human Serpin Peptidase Inhibitor, Clade G Member 1 produced in Human plasma having a molecular mass of 110 kDa.

Source

Human Plasma.

Formulation

10mM sodium phosphate and 145mM NaCl, pH 7.3.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. SERPING1 is also activating C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.
Synonyms
C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.
Physical Appearance
Sterile Filtered solution.
Stability
Native SERPING1 Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1,HIV-2, HCV, HTLV-I &II, STS and HBSAG.

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:

Listeriolysin-O Recombinant

Listeriolysin-O, LLO, hlyA.

Product # :

PRO-320

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Description

LLO is a single, non-glycosylated polypeptide chain containing 529 amino acids and having a molecular mass of 58kDa. (accession number: AAF64524).

Source

Escherichia Coli.

Formulation

The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, pH 6.4, 1mM DTT, 5% (v/v) glycerol and 0.5M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Hemolytic activity is 8,27E+05 HU/mg of protein where HU means hemolytic activity unit that is the amount of toxin needed to release half the hemoglobin (50% lysis) of the erythrocytes as determined by hemolysin assay.

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Introduction
Listeriolysin O (aka LLO) is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene and composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents and inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes (average pH ~ 5.9) of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, and the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system and antibodies. LLO also brings about dephosphorylation of histone H3 and deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO and is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST's supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO.
Synonyms
Listeriolysin-O, LLO, hlyA.
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.

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:

Transferrin Human Recombinant, CHO

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

Product # :

PRO-2782

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Description

Recombinant Human Transferrin produced in CHO cells is a glycosylated, polypeptide chain containing having a molecular mass of 76 kDa. Human Transferrin has homologous C and N-terminal domains, each of which binds one ion of ferric iron.

Source

Chinese Hamster Ovary cells.

Formulation

Transferrin solution contains 0.05% NaN3 and PBS.

Purity

Protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
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.
Applications
Immunoassay, cell culture.
Background
Human recombinant transferrin, a glycoprotein responsible for iron transport in the body, has gained increasing attention in the fields of biomedicine and health sciences. This multifaceted protein serves as an essential carrier of iron and is crucial for cellular growth, immunity, and various physiological processes. Its recombinant form, produced through advanced biotechnological methods, offers several advantages for therapeutic and research purposes. This study aims to provide a comprehensive exploration of human recombinant transferrin, shedding light on its various functions and potential applications in health and biomedicine.
The primary objective of this research is to elucidate the essential role of transferrin in iron homeostasis and its significance for human health. In vitro and in vivo experiments will be conducted to investigate how recombinant transferrin interacts with cellular receptors, regulates iron uptake, and influences cellular proliferation. Understanding these mechanisms is fundamental for deciphering the complexities of iron metabolism and its impact on health and disease.
The second objective is to assess the clinical relevance of human recombinant transferrin in medical interventions. Clinical trials and studies involving individuals with iron-related disorders, such as iron-deficiency anemia, will be conducted to evaluate the efficacy and safety of recombinant transferrin supplementation. These investigations may provide insights into the use of recombinant transferrin as a therapeutic agent in various clinical settings.
The third objective is to explore the broader implications of human recombinant transferrin in biomedicine and research. Research will investigate its potential roles in areas beyond iron transport, such as drug delivery, tissue engineering, and cell culture. Understanding the multifaceted properties of recombinant transferrin may open new avenues for innovative approaches in various medical specialties and scientific research.
By delving into the diverse functions of human recombinant transferrin, this research aims to expand our understanding of its physiological roles and clinical applications. The findings may contribute to the development of innovative strategies for the treatment of iron-related disorders and the advancement of biomedicine and scientific research.

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:

HIV-2 gp32 Recombinant, Biotin Labeled

Product # :

HIV-135

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Description

HIV-2 gp32 Biotin Labeled recombinant- contains the full-length sequence of HIV-2 envelope immunodominant regions gp32 having a Mw of 32kDa and fused to a beta-galactosidase at N-terminus.

Source

Escherichia Coli.

Formulation

0.01M Na2CO3, 10mM EDTA, 14mM beta-ME and 0.02% Sarcosyl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
HIV-1 and HIV-2 appear to package their RNA differently. HIV-1 binds to any appropriate RNA whereas HIV-2 preferentially binds to mRNA which creates the Gag protein itself. This means that HIV-1 is better able to mutate. HIV-2 is transmitted in the same ways as HIV-1: Through exposure to bodily fluids such as blood, semen, tears and vaginal fluids.
Immunodeficiency develops more slowly with HIV-2.
HIV-2 is less infectious in the early stages of the virus than with HIV-1.
The infectiousness of HIV-2 increases as the virus progresses.
Major differences include reduced pathogenicity of HIV-2 relative to HIV-1, enhanced immune control of HIV-2 infection and often some degree of CD4-independence. Despite considerable sequence and phenotypic differences between HIV-1 and 2 envelopes, structurally they are quite similar. Both membrane-anchored proteins eventually form the 6-helix bundles from the N-terminal and C-terminal regions of the ectodomain, which is common to many viral and cellular fusion proteins and which seems to drive fusion.
HIV-1 gp41 helical regions can form more stable 6-helix bundles than HIV-2 gp41 helical regions however HIV-2 fusion occurs at a lower threshold temperature (25°C), does not require Ca2+ in the medium, is insensitive to treatment of target cells with cytochalasin B, and is not affected by target membrane glycosphingolipid composition.
Physical Appearance
Sterile filtered colorless clear solution.
Stability
HIV-2 gp-32 although stable at room temperature for 3 weeks, should be stored at 4°C.

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:

Noggin Human Recombinant

SYM1, SYNS1, NOG.

Product # :

CYT-475

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Description

Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED₅₀ for this effect is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x10⁵units/mg.

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Introduction
The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.
Synonyms
SYM1, SYNS1, NOG.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.
Amino Acid Sequence
MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC.
Background
Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.
Abstract:
Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.
Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.
This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.
Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
1. Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.
Molecular Characteristics of Noggin :
1. This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.
Inhibition of BMP Signaling by Noggin:
1. Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.
Physiological Functions of Noggin:
1. Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.
Therapeutic Implications of Noggin:
1. The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.
Clinical Studies and Translational Research:
1. This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical studies.

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:

Angiopoietin-like Protein 2 Human Recombinant

Angiopoietin-related protein 2, Angiopoietin-like protein 2, ANGPTL2, ARP2, HARP.

Product # :

CYT-765

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sds-page

Description

ANGPTL2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 493 amino acids ( 22-493 a.a.) including a 20 a.a N-terminal His tag. The total molecular mass is 57.1kDa (calculated).

Source

Escherichia Coli.

Formulation

ANGPTL2 protein solution (0.5mg/ml) contains 20mM Tris HCL (pH7-8) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

sds-page

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Introduction
Angiopoietins belong to the vascular endothelial growth factor family and the only known growth factors largely specific for vascular endothelium. Angiopoietins-1, 2 and 4 partake in the formation of blood vessels. ANGPTL2 displays angiogenic effects. Angiopoietin-like Protein 2 (ANGPTL2) is an anti-diabetic factor. ANGPTL2 induces sprouting in endothelial cells through an autocrine and paracrine action. ANGPTL2 increases insulin sensitivity in adipocytes. In addition, ANGPTL2 is a mediator of chronic adipose tissue inflammation. ANGPTL2 is widely expressed in the heart, small intestine, spleen and stomach. ANGPTL2 is also found in lower levels in the colon, ovary, adrenal gland, skeletal muscle and in prostate.
Synonyms
Angiopoietin-related protein 2, Angiopoietin-like protein 2, ANGPTL2, ARP2, HARP.
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 MGQEDGFEGT EEGSPREFIY LNRYKRAGES QDKCTYTFIV PQQRVTGAIC VNSKEPEVLL ENRVHKQELE LLNNELLKQK RQIETLQQLV EVDGGIVSEV KLLRKESRNM NSRVTQLYMQ LLHEIIRKRD NALELSQLEN RILNQTADML QLASKYKDLE HKYQHLATLA HNQSEIIAQL EEHCQRVPSA RPVPQPPPAA PPRVYQPPTY NRIINQISTN EIQSDQNLKV LPPPLPTMPT LTSLPSSTDK PSGPWRDCLQ ALEDGHDTSS IYLVKPENTN RLMQVWCDQR HDPGGWTVIQ RRLDGSVNFF RNWETYKQGF GNIDGEYWLG LENIYWLTNQ GNYKLLVTME DWSGRKVFAE YASFRLEPES EYYKLRLGRY HGNAGDSFTW HNGKQFTTLD RDHDVYTGNC AHYQKGGWWY NACAHSNLNG VWYRGGHYRS RYQDGVYWAE FRGGSYSLKK VVMMIRPNPN TFH
Background
Angiopoietin-like Protein 2 Human Recombinant: A Potential Therapeutic Target for Metabolic and Cardiovascular Disorders
Abstract:
Angiopoietin-like protein 2 (ANGPTL2) has emerged as a crucial regulator in metabolic and cardiovascular disorders. This multifunctional protein is involved in various biological processes, including angiogenesis, adipose tissue function, and inflammation. The availability of human recombinant ANGPTL2 protein has provided researchers with a valuable tool to explore its therapeutic potential. This concise review provides an overview of the role of ANGPTL2 in metabolic and cardiovascular health and discusses the potential of ANGPTL2 human recombinant protein as a therapeutic target.
Introduction:
Metabolic disorders, such as obesity and type 2 diabetes, are closely associated with cardiovascular diseases and pose significant global health challenges. ANGPTL2, a member of the angiopoietin-like protein family, has gained attention for its involvement in metabolic regulation and cardiovascular homeostasis. Through interactions with various receptors and signaling pathways, ANGPTL2 influences lipid metabolism, insulin sensitivity, inflammation, and vascular integrity.
Mechanisms of ANGPTL2 Action:
ANGPTL2 acts through binding to integrins, toll-like receptors (TLRs), and other receptors on different cell types, including adipocytes, endothelial cells, and immune cells. By influencing angiogenesis, inflammation, and extracellular matrix remodeling, ANGPTL2 affects adipose tissue function, lipid metabolism, and insulin signaling.
Role of ANGPTL2 in Metabolic Regulation:
ANGPTL2 plays a critical role in metabolic regulation and the development of metabolic disorders. It promotes adipose tissue inflammation, impairs adipogenesis, and alters adipokine secretion, contributing to metabolic dysfunction. Furthermore, ANGPTL2 modulates lipid metabolism by regulating lipoprotein lipase activity, affecting triglyceride clearance, and promoting hepatic lipid accumulation.
ANGPTL2 in Cardiovascular Health and Disease:
Increasing evidence suggests that ANGPTL2 is implicated in cardiovascular diseases, including atherosclerosis and heart failure. ANGPTL2 promotes vascular inflammation, endothelial dysfunction, and smooth muscle cell proliferation, which contribute to atherosclerotic plaque progression and vascular remodeling. Additionally, ANGPTL2 influences cardiac remodeling and fibrosis, impacting heart failure development.
Therapeutic Potential of ANGPTL2 Human Recombinant Protein:
The availability of ANGPTL2 human recombinant protein opens avenues for therapeutic interventions targeting metabolic and cardiovascular disorders. Preclinical studies employing ANGPTL2 blockade or supplementation have shown promising results in improving metabolic parameters, reducing atherosclerosis, and preserving cardiac function. However, further research is needed to optimize the clinical application of ANGPTL2 human recombinant protein, including dosage, timing, and delivery methods.
Conclusion:
ANGPTL2 holds promise as a therapeutic target for metabolic and cardiovascular disorders. Its involvement in key biological processes makes it an attractive candidate for interventions aiming to improve metabolic health and prevent cardiovascular complications. The development of ANGPTL2 human recombinant protein provides a valuable tool for investigating its therapeutic potential further.
What is the molecular weight/Mw of ANGPTL2 Protein?
ANGPTL2 Protein has a total Mw of 57.1kDa.

What is the source or expression system of ANGPTL2 Protein?
Escherichia Coli.

What is the Purity of ANGPTL2 Protein?
ANGPTL2 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of ANGPTL2 Protein?
The biological functionality of ANGPTL2 Protein will be determined in the future.

What is the amino acid sequence of ANGPTL2 Protein?
MGSSHHHHHH SSGLVPRGSH MGQEDGFEGT EEGSPREFIY LNRYKRAGES QDKCTYTFIV PQQRVTGAIC VNSKEPEVLL ENRVHKQELE LLNNELLKQK RQIETLQQLV EVDGGIVSEV KLLRKESRNM NSRVTQLYMQ LLHEIIRKRD NALELSQLEN RILNQTADML QLASKYKDLE HKYQHLATLA HNQSEIIAQL EEHCQRVPSA RPVPQPPPAA PPRVYQPPTY NRIINQISTN EIQSDQNLKV LPPPLPTMPT LTSLPSSTDK PSGPWRDCLQ ALEDGHDTSS IYLVKPENTN RLMQVWCDQR HDPGGWTVIQ RRLDGSVNFF RNWETYKQGF GNIDGEYWLG LENIYWLTNQ GNYKLLVTME DWSGRKVFAE YASFRLEPES EYYKLRLGRY HGNAGDSFTW HNGKQFTTLD RDHDVYTGNC AHYQKGGWWY NACAHSNLNG VWYRGGHYRS RYQDGVYWAE FRGGSYSLKK VVMMIRPNPN TFH

What applications can ANGPTL2 Protein be used in?
ANGPTL2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ANGPTL2 Protein?
The endotoxin level is minimal, ANGPTL2 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:

FAS Blocking/Activating antibody (CD95), Mouse anti Human

FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95, Tumor necrosis factor receptor superfamily member 6 TNR6, APT1, FAS1, TNFRSF6.

Product # :

ANT-204

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Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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Formulation

1 mg/ml in PBS (after reconstitution).

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Introduction
The Fas receptor (CD95) mediates apoptotic signaling by Fas-ligand expressed on the surface of other cells. The Fas-FasL interaction plays an important role in the immune system and lack of this system leads to autoimmunity, indicating that Fas-mediated apoptosis removes self-reactive lymphocytes. Fas signaling is also involved in immune surveillance to remove transformed cells and virus infected cells. Binding of FAS to oligimerized FasL on another cell activates apoptotic signaling through a cytoplasmic domain termed the death domain that interacts with signaling adaptors including FAF, FADD and DAX to activate the caspase proteolytic cascade. Caspase-8 and caspase-10 are first activated, to then cleave and activate downstream caspases, and a variety of cellular substrates that lead to cell death. Caspases cleave nuclear lamins, causing the nucleus to break down and lose its normal structure and another caspase substrate is DFF, inducing cleavage and degradation of the genome. Other caspase substrates are involved in cytoskeletal structure, cell cycle regulation and signaling pathways. Activation of JNK kinase, activation of Jun, and production of ceramide may also play roles in Fas-mediated apoptosis. Activation of fas-mediated apoptosis is opposed by I-FLICE and FAP. Viruses and tumors may escape immune surveillance in part through suppression of fas-mediated apoptosis using similar mechanisms.
Synonyms
FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95, Tumor necrosis factor receptor superfamily member 6 TNR6, APT1, FAS1, TNFRSF6.
Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
Recombinant Human FAS.
Ig Subclass
mouse IgG1.
Clone
NYRhFAS.
Note
This antibody is a BLOCKING antibody when in soluble form and will block FAS-mediated apoptosis. It will ACTIVATE FAS-mediated killing when immobilized.
Titer
By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Protein-A column.

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:

LY6G, Rat Anti Mouse Antibody, Biotin

Lymphocyte antigen 6G, Ly-6G, Ly-6G.1, Ly6g, Gr1, Gr-1.

Product # :

ANT-074

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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formulation
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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
Myeloid differentiation antigen Gr1 (Ly6G) is a GPI-anchored protein, which is briefly expressed on monocytes in the bone marrow. The level of the Ly6G expression in the bone marrow completely correlates with granulocyte differentiation and maturation. Ly6G ligation on murine neutrophils inhibits neutrophil recruitment, thus providing the first evidence of a function for the Ly6G molecule. Ly6G is seen primarily on neutrophils, also in a subgroup of eosinophils, differentiating pre-monocytes and plasmacytoid dendritic cells.
Synonyms
Lymphocyte antigen 6G, Ly-6G, Ly-6G.1, Ly6g, Gr1, Gr-1.
Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
Ly-6G-transfected cell line.
Ig Subclass
Rat IgG2a.
Clone
YRmLy-6G.
Applications
Flow cytometry, immunohistochemistry, cell depletion.
This antibody recognizes only Ly-6G which is expressed on most myeloid cells in the bone marrow and all peripheral granulocytes. For flow cytometry, use 10 µl/106 cells. Exact titer for cell depletion in vivo (cytotoxicity) should be determined by the investigator.
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Available Conjugates
This antibody is also available unconjugated and conjugated to FITC.
Type
Rat Anti Mouse Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Protein A column.

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:

Aminoacyl tRNA Synthetase Complex-Interacting Multifunctional Protein 1 Human Recombinant

Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.

Product # :

CYT-021

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Quantity :

Shipping Method :

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source
formulation
purity
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sds-page

Description

AIMP1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 356 amino acids (1-336 a.a.) and having a molecular mass of 39.2kDa (Molecular size on SDS-PAGE will appear higher). The AIMP1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The AIMP1 solution (0.25mg/ml) 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

sds-page

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Introduction
AIMP1 (EMPA2 or p43) is a cytokine that is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of the AIMP1 cytokine renders the tumor-associated vasculature sensitive to tumor necrosis factor. Furthermore, AIMP1 is involved in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
Synonyms
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1, Multisynthase complex auxiliary component p43, AIMP1, EMAP2, SCYE1, p43, EMAPII.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLPAVAVSEP VVLRFMIFCR LLAKMANNDA VLKRLEQKGA EADQIIEYLK QQVSLLKEKA ILQATLREEK KLRVENAKLK KEIEELKQEL IQAEIQNGVK QIPFPSGTPL HANSMVSENV IQSTAVTTVS SGTKEQIKGG TGDEKKAKEK IEKKGEKKEK KQQSIAGSAD SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
Background
What is the molecular weight/Mw of AIMP1 HUMAN Protein?
AIMP1 HUMAN Protein has a total Mw of 39.2kDa.

What is the source or expression system of AIMP1 HUMAN Protein?
Escherichia Coli.

What is the Purity of AIMP1 HUMAN Protein?
AIMP1 HUMAN Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of AIMP1 HUMAN Protein?
The biological functionality of AIMP1 HUMAN Protein will be determined in the future.

What is the amino acid sequence of AIMP1 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MLPAVAVSEP VVLRFMIFCR LLAKMANNDA VLKRLEQKGA EADQIIEYLK QQVSLLKEKA ILQATLREEK KLRVENAKLK KEIEELKQEL IQAEIQNGVK QIPFPSGTPL HANSMVSENV IQSTAVTTVS SGTKEQIKGG TGDEKKAKEK IEKKGEKKEK KQQSIAGSAD SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQMQNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

What applications can AIMP1 HUMAN Protein be used in?
AIMP1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for AIMP1 HUMAN Protein?
The endotoxin level is minimal, AIMP1 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:

Angiopoietin 2 Human Recombinant

Angiopoietin-2, Angiopoietin2, ANGPT2, ANG2, ANG-2, ANGPT-2.

Product # :

CYT-1103

Price :

Quantity :

Shipping Method :

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source
formulation
purity
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sds-page

Description

ANGPT2 produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a single, polypeptide chain (19-496 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 484 amino acids and having a molecular mass of 55.7kDa.ANGPT2 shows multiple bands between 50-100kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Chinese Hamster Ovary Cells (CHO).

Formulation

ANGPT2 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

sds-page

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Introduction
ANGPT2 aka Angiopoietin-2 competes for binding to the TIE2 receptor and blocks angiopoietin-1 aka ANGPT1 induced TIE2 autophosphorylation during vasculogenesis. ANGPT-2 is a naturally occurring antagonist of ANGPT-1. ANGPT2 induces tyrosine phosphorylation of TEK/TIE2 in the lack of Angiopoietin-2. In the deficiency of VEGF an angiogenic inducer, ANGPT-2 induces endothelial cell apoptosis resulting in vascular regression. ANGPT2 along with VEGF enable endothelial cell migration and proliferation, resulting in permissive angiogenic signal.
Synonyms
Angiopoietin-2, Angiopoietin2, ANGPT2, ANG2, ANG-2, ANGPT-2.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
YNNFRKSMDS IGKKQYQVQH GSCSYTFLLP EMDNCRSSSS PYVSNAVQRD APLEYDDSVQ
RLQVLENIME NNTQWLMKLE NYIQDNMKKEMVEIQQNAVQ NQTAVMIEIG TNLLNQTAEQ
TRKLTDVEAQ VLNQTTRLEL QLLEHSLSTN KLEKQILDQT SEINKLQDKN
SFLEKKVLAMEDKHIIQLQS IKEEKDQLQV LVSKQNSIIE ELEKKIVTAT VNNSVLQKQQ
HDLMETVNNL LTMMSTSNSA KDPTVAKEEQ ISFRDCAEVFKSGHTTNGIY TLTFPNSTEE
IKAYCDMEAG GGGWTIIQRR EDGSVDFQRT WKEYKVGFGN PSGEYWLGNE FVSQLTNQQR
YVLKIHLKDWEGNEAYSLYE HFYLSSEELN YRIHLKGLTG TAGKISSISQ PGNDFSTKDG
DNDKCICKCS QMLTGGWWFD ACGPSNLNGM YYPQRQNTNKFNGIKWYYWK GSGYSLKATT MMIRPADFHH HHHH
Background
6. Therapeutic Implications of Ang-2
Given its critical role in angiogenesis and its involvement in various disease states, Ang-2 represents a promising target for therapeutic interventions. Strategies aimed at modulating Ang-2 signaling, such as the development of neutralizing antibodies or small molecule inhibitors, hold great potential for managing angiogenesis-related disorders and improving patient outcomes.
7. Conclusion and Future Perspectives
Our understanding of Ang-2 and its multifaceted involvement in angiogenesis has advanced significantly. However, further research is required to elucidate the complex interplay between Ang-2 and other angiogenic factors, as well as to explore the potential of Ang-2-targeted therapies. Continued investigations will pave the way for the development of innovative treatment approaches for angiogenesis-related disorders, ultimately improving patient care.
What is the molecular weight/Mw of ANGPT2 Protein?
ANGPT2 Protein has a total Mw of 55.7kDa.

What is the source or expression system of ANGPT2 Protein?
Chinese Hamster Ovary Cells

What is the Purity of ANGPT2 Protein?
ANGPT2 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of ANGPT2 Protein?
The biological functionality of ANGPT2 Protein will be determined in the future.

What is the amino acid sequence of ANGPT2 Protein?
YNNFRKSMDS IGKKQYQVQH GSCSYTFLLP EMDNCRSSSS PYVSNAVQRD APLEYDDSVQ
RLQVLENIME NNTQWLMKLE NYIQDNMKKEMVEIQQNAVQ NQTAVMIEIG TNLLNQTAEQ
TRKLTDVEAQ VLNQTTRLEL QLLEHSLSTN KLEKQILDQT SEINKLQDKN
SFLEKKVLAMEDKHIIQLQS IKEEKDQLQV LVSKQNSIIE ELEKKIVTAT VNNSVLQKQQ
HDLMETVNNL LTMMSTSNSA KDPTVAKEEQ ISFRDCAEVFKSGHTTNGIY TLTFPNSTEE
IKAYCDMEAG GGGWTIIQRR EDGSVDFQRT WKEYKVGFGN PSGEYWLGNE FVSQLTNQQR
YVLKIHLKDWEGNEAYSLYE HFYLSSEELN YRIHLKGLTG TAGKISSISQ PGNDFSTKDG
DNDKCICKCS QMLTGGWWFD ACGPSNLNGM YYPQRQNTNKFNGIKWYYWK GSGYSLKATT MMIRPADFHH HHHH

What applications can ANGPT2 Protein be used in?
ANGPT2 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ANGPT2 Protein?
The endotoxin level is minimal, ANGPT2 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:

Sparc/Osteonectin 3 Mouse Recombinant

Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.

Product # :

PRO-2328

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Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
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Description

SPOCK3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 423 amino acids (22-436 a.a.) and having a molecular mass of 47.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).SPOCK3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

SPOCK3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Testican-3 (Spock3) is a nervous system-expressed heparan sulfate proteoglycan belonging to a subgroup of the BM-40/SPARC/osteonectin family, whose role of in brain development is unclear. Spock3 inhibits the processing of pro-matrix metalloproteinase 2(MMP-2) by MT1-MMP and MT3-MMP. Spock3 is mostly confined to the developmental stage of the brain.
Synonyms
Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.
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
AAAAVAVAGG RSDGGNFLDE KQWLTTISQY DKEVGQWNKF RDEVEDDYFR TWNPGKPFDQ ALDPAKDPCL KTKCSRHKVC ITQDAQTALC ISHRRLTHSM KEVGGSHKQW RGLPSSTCKP CPIAYASPVC GSDGHSYSSQ CKLEYQACVL GKQISIKCEG RCPCPSDKSM NIGRNVKRAC
SDLEFREVAN RLRDWFKALH ESGSQNKKTK ALLRPERSRF DTSILPICKD SLGWMFNRLD TNYDLLLDQS ELGSIYLDKN EQCTKAFFNS CDTYKDSLIS NNEWCYCFQR QQDPPCHTEL SNIQKRQGIK KLLGQYIPLC DEDGYYKPTQ CHGSVGQCWC VDRYGNEVVG SRINGVADCA
IDFEISGDFA SGDFREWTDD EGEEDDIMND KDDIEDDDED EGDDDDDGDV HDGYILEHHH HHH

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

Description:

Interleukin-6 Rat Recombinant, sf9

IL6, Ifnb2, ILg6.

Product # :

CYT-1048

Price :

Quantity :

Shipping Method :

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source
formulation
purity
biological activity
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Description

IL6 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 196 amino acids (25-211 a.a.) and having a molecular mass of 22.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-28 kDa).IL6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL6 protein solution (0.5mg/ml) contains 20% glycerol & Phosphate Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using M-NFS-60 mouse B cell. The ED50 for this effects is less or equal to 0.1 ng/ml.

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Introduction
Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.
Synonyms
IL6, Ifnb2, ILg6.
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
ADPFPTSQVR RGDFTEDTTH NRPVYTTSQV GGLITYVLRE ILEMRKELCN GNSDCMNSDDALSENNLKLP EIQRNDGCFQ TGYNQEICLL KICSGLLEFR FYLEFVKNNL QDNKKDKARVIQSNTETLVH IFKQEIKDSY KIVLPTPTSN ALLMEKLESQ KEWLRTKTIQ LILKALEEFL KVTMRSTRQT HHHHHH
Background
Production and Applications of Rat Recombinant Interleukin-6 in sf9 Cells
Abstract:
Interleukin-6 (IL-6) is a critical cytokine involved in various physiological processes, including inflammation, immune responses, and hematopoiesis. The production of recombinant IL-6 has paved the way for numerous applications in research and therapeutic development. This paper elucidates the production of Rat Recombinant IL-6 in sf9 cells using baculovirus expression system and explores its potential applications in immunology and disease research.
Introduction:
Interleukin-6 is a pleiotropic cytokine with diverse functions in immune regulation, acute phase responses, and tissue homeostasis. The ability to produce recombinant IL-6 allows researchers to investigate its role in various biological contexts and develop potential therapies. The sf9 cell line, derived from Spodoptera frugiperda insect cells, offers an efficient platform for recombinant protein expression through the baculovirus system.
Methods:
The production of Rat Recombinant IL-6 involves inserting the rat IL-6 gene into a baculovirus transfer vector. This vector is then co-transfected with a linearized baculovirus DNA into sf9 cells. The resulting recombinant baculovirus expresses the IL-6 protein, which is secreted into the culture medium. The expressed protein is subsequently purified using chromatographic techniques to ensure its quality and activity.
Applications:
Rat Recombinant IL-6 produced in sf9 cells has widespread applications. It serves as a valuable tool for investigating the mechanisms underlying IL-6-mediated immune responses, inflammation, and hematopoiesis. Furthermore, it enables the development of potential therapies targeting IL-6-related disorders, including autoimmune diseases, inflammatory conditions, and certain types of cancer.
Advantages of sf9 Expression:
The sf9 expression system offers several advantages, including high protein yields, post-translational modifications, and proper protein folding. This system is especially suitable for complex cytokines like IL-6, which require correct tertiary structure for optimal biological activity.
Challenges and Future Prospects:
While sf9-based expression of Rat Recombinant IL-6 offers numerous benefits, challenges such as optimization of expression conditions, scale-up, and quality control remain. Additionally, further research is needed to explore the therapeutic potential of Rat Recombinant IL-6 in preclinical and clinical settings.
Conclusion:
The production of Rat Recombinant IL-6 in sf9 cells using the baculovirus expression system provides a powerful tool for unraveling the roles of IL-6 in various biological processes. This platform holds promise for advancing our understanding of IL-6-related diseases and facilitating the development of targeted 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:

Jun Proto-Oncogene (1-241 a.a.) Human Recombinant

Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.

Product # :

PKA-001

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Quantity :

Shipping Method :

Shipped with Ice Packs

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source
formulation
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Description

C-JUN Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 261 amino acids (1-241 a.a.) and having a molecular mass of 27.3kDa. The C-JUN is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The C-JUN solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
C-JUN is a gene which, in combination with c-Fos, forms the AP-1early response transcription factor. C-JUN is activated by the JNKpathway. C-JUN is the putative transforming gene of avian sarcoma virus 17. C-JUN is a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. The C-JUN gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.
Synonyms
Transcription factor AP-1, Activator protein 1, AP1, Proto-oncogene c-jun, V-jun avian sarcoma virus 17 oncogene homolog, p39, c-Jun.
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 MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP P.

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:

Interleukin-4 Receptor Human Recombinant

Interleukin 4 Receptor, IL-4 Receptor Subunit Alpha, Interleukin 13 Receptor, IL-4RA, IL4RA, Interleukin-4 Receptor Subunit Alpha, Interleukin-4 Receptor Alpha Chain, IL4R Nirs Variant 1, IL-4R Subunit Alpha, CD124 Antigen, IL-4R-Alpha, CD124, IL4R.

Product # :

CYT-1047

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Description

IL4R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (26-232 a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 215 amino acids and having a molecular mass of 24.7kDa.IL4R shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL4R protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
Synonyms
Interleukin 4 Receptor, IL-4 Receptor Subunit Alpha, Interleukin 13 Receptor, IL-4RA, IL4RA, Interleukin-4 Receptor Subunit Alpha, Interleukin-4 Receptor Alpha Chain, IL4R Nirs Variant 1, IL-4R Subunit Alpha, CD124 Antigen, IL-4R-Alpha, CD124, IL4R.
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
MKVLQEPTCV SDYMSISTCE WKMNGPTNCS TELRLLYQLV FLLSEAHTCI PENNGGAGCV CHLLMDDVVS ADNYTLDLWA GQQLLWKGSF KPSEHVKPRA PGNLTVHTNV SDTLLLTWSN PYPPDNYLYN HLTYAVNIWS ENDPADFRIY NVTYLEPSLR IAASTLKSGI SYRARVRAWA
QCYNTTWSEW SPSTKWHNSY REPFEQHLEH HHHHH

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:

Protein A/G Recombinant, His Tag

Product # :

PRO-1927

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Description

Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 3 of protein G (C1-C2-C3) containing 513 amino acids in total and having a molecular mass of 56.9kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

Source

Escherichia Coli.

Formulation

Protein-A/G was lyophilized without any additives.

Purity

Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
The recombinant Protein A/G is a genetically engineered protein comprised of 8 IgG-binding domains EDABC-C1C2C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1, C2 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Protein-A/G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G 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 Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE KLAAALEHHH HHH.

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

Description:

Insulin-Like Growth Factor Binding Protein-1 Human Recombinant

IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.

Product # :

CYT-299

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Description

IGFBP-1 Human Recombinant (26-259 a.a.) produced in NS0 is a single, glycosylated, polypeptide chain containing 234 amino acids and having a molecular mass of 25kDa. The IGFBP1 is purified by proprietary chromatographic techniques.

Source

Mouse myeloma cell line, NS0.

Formulation

IGFBP-1 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as determined by the inhibition of rHuIGF-I-induced proliferation of human MCF-7 cells, is less than 4µg/ml.

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Introduction
IGFBP1 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Synonyms
IBP-1, IGF-Binding Protein 1, AFBP, PP12, IGF-BP25, hIGFBP-1, IGFBP-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IGFBP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF-BP1 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 IBP-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.
Background
What is the molecular weight/Mw of IGFBP1 HUMAN Protein?
IGFBP1 HUMAN Protein has a total Mw of 25kDa.

What is the source or expression system of IGFBP1 HUMAN Protein?
Mouse myeloma cell line, NS0.

What is the Purity of IGFBP1 HUMAN Protein?
IGFBP1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IGFBP1 HUMAN Protein?
The ED50, as determined by the inhibition of rHuIGF-I-induced proliferation of human MCF-7 cells, is less than 4µg/ml.

What is the amino acid sequence of IGFBP1 HUMAN Protein?
APWQCAPCSA EKLALCPPVS ASCSEVTRSA GCGCCPMCAL PLGAACGVAT ARCARGLSCR ALPGEQQPLH ALTRGQGACV QESDASAPHA AEAGSPESPE STEITEEELL DNFHLMAPSE EDHSILWDAI STYDGSKALH VTNIKKWKEP CRIELYRVVE SLAKAQETSG EEISKFYLPN CNKNGFYHSR QCETSMDGEA GLCWCVYPWN GKRIPGSPEI RGDPNCQIYF NVQN.

What applications can IGFBP1 HUMAN Protein be used in?
IGFBP1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IGFBP1 HUMAN Protein?
The endotoxin level is minimal, IGFBP1 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:

Ebola Zaire Glycoprotein Recombinant

Product # :

EVD-077

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Description

Recombinant Ebola Zaire Glycoprotein is a mucin like domain containing 181 amino acids was derived from Zaire Ebola Virus (strain Kikwit-95) gp mucin sequence produced in E. coli, and fused to a 6xHis tag at its C-terminus, having a molecular weight 38kDa.Ebola Zaire GP is purified by a proprietary chromatographic technique.

Source

Escherichia Coli.

Formulation

Ebola Zaire GP protein solution is supplied in Phosphate buffer with 25mM arginine and 0.02% sodium azide.

Purity

>95% pure as determined by 12% SDS-PAGE (Coomassie blue stain).

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Introduction
Ebolavirus (EVD) belongs to the Filoviridae family of proteins which is comprised of a single-strand, non-infectious RNA genome. EVD genome is about 19,000 base pairs long and covers 7 genes in the order 3'-UTR-NP-VP35-VP40-GP-VP30-VP24-L-5'-UTR. There are 4 different ebolaviruses such as: Zaire (EBO-Z), Sudan (EBO-S), Cote d’Ivoire (EBO-CI) and Reston (EBO-R) that differ in amino acid sequence and location of where the gene overlaps. The EBOV glycoprotein is the only virally expressed protein above the virion surface. The EBOV glycoprotein is essential for virus attachment to host cell and fusion with target cell. Mucin like domain within Ebola virus glycoprotein contains multiple glycosylated amino acids. It has been shown that antibodies frequently develop against its mucin like domain. Recombinant mucin like domain is a suitable antigen to test specific antibodies from Ebola virus infected patients.
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.
Applications
Immunoassay.

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:

HSA Human Protein

HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

Product # :

PRO-354

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Description

HSA contains 584 amino acid residues derived from the prototypicalHSA sequence.

Source

Human Serum.

Formulation

0.2gr/ml solution containing no additives.

Purity

Greater than 97.0% as determined by SDS-PAGE.

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Introduction
HSA is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted HSA. HSA is a soluble, monomeric protein which comprises about one-half of the blood serum protein. HSA functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. HSA is a globular unglycosylated serum protein of molecular weight 65,000. The human HSA gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.
Suitable for use in biochemical, excipient (an inert substance used as a diluent or vehicle for a drug), culture media and chromatographic applications.
Synonyms
HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Physical Appearance
Sterile Filtered clear yellowish solution.
Stability
HSA although stable at room temperature for 2 weeks should be stored at 4°C.

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:

Chitinase 3-Like 2, Mouse Anti Human

Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, CHI3L2.

Product # :

ANT-703

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formulation
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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
Chitinase 3-Like 2 (CHI3L2) is similar to bacterial chitinases but lacks chitinase activity. CHI3L2 protein is secreted and is involved in cartilage biogenesis. CHI3L2 is a lectin, which binds chitooligosaccharides and other glycans with high affinity, but not heparin.
Synonyms
Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, CHI3L2.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human CHI3L2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CHI3L2 amino acids 27-390 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
PAT2B5AT.
Applications
CHI3L2 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
CHI3L2 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

Description:

Beta Defensin 116 Human Recombinant

Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.

Product # :

CYT-713

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Description

DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

sds-page

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Introduction
Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.
Synonyms
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
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 MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
Background
Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications
Abstract:

Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.
Introduction:

Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.
Production and Characterization:

Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.
Antimicrobial Properties:

BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.
Therapeutic Implications:

The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.
Conclusion:

Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.
What is the molecular weight/Mw of DEFB116 Protein?
DEFB116 Protein has a total Mw of 11.5kDa.

What is the source or expression system of DEFB116 Protein?
Escherichia Coli.

What is the Purity of DEFB116 Protein?
DEFB116 Protein is >80% pure as determined by SDS-PAGE.

What is the Biological Activity of DEFB116 Protein?
The biological functionality of DEFB116 Protein will be determined in the future.

What is the amino acid sequence of DEFB116 Protein?
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.

What applications can DEFB116 Protein be used in?
DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for DEFB116 Protein?
The endotoxin level is minimal, DEFB116 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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